1653
Pathway
N-Oxide Electron Transfer
The pathway can start in various spots. First step in this case starts with NADH interacting with a menaquinone oxidoreductase resulting in the release of a NADH and a hydrogen Ion, at the same time in the inner membrane a menaquinone interacts with 2 electrons and 2 hydrogen ions thus releasing a menaquinol. This allows for 4 hydrogen ions to be transferred from the cytosol to the periplasmic space. The menaquinol then interacts with a trimethylamine N-oxide reductase resulting in the release of 2 hydrogen ion and 2 electrons. At the same time trimethylamine N-oxide and 3 hydrogen ions interact with the enzyme trimethylamine N-oxide reductase resulting in the release of a trimethylamine and a water molecule, this reaction happening in the periplasmic space.
The second set of reactions starts with a hydrogen interacting with a menaquinone oxidoreductase resulting in the release of two electrons being released into the inner membrane which then react with with 2 hydrogen ion and a menaquinone to produce a menaquinol. This menaquinol then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before.
The third set of reactions starts with with formate interacting with a formate dehydrogenase-O resulting in a release of carbon dioxide and a hydrogen ion, this releases 2 electrons that interact with a menaquinone and two hydrogen ions. This releases a menaquinol which then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before
Metabolic
PW001889
Center
PathwayVisualizationContext2176
2134
3002
#000099
PathwayVisualization1637
1653
N-Oxide Electron Transfer
The pathway can start in various spots. First step in this case starts with NADH interacting with a menaquinone oxidoreductase resulting in the release of a NADH and a hydrogen Ion, at the same time in the inner membrane a menaquinone interacts with 2 electrons and 2 hydrogen ions thus releasing a menaquinol. This allows for 4 hydrogen ions to be transferred from the cytosol to the periplasmic space. The menaquinol then interacts with a trimethylamine N-oxide reductase resulting in the release of 2 hydrogen ion and 2 electrons. At the same time trimethylamine N-oxide and 3 hydrogen ions interact with the enzyme trimethylamine N-oxide reductase resulting in the release of a trimethylamine and a water molecule, this reaction happening in the periplasmic space.
The second set of reactions starts with a hydrogen interacting with a menaquinone oxidoreductase resulting in the release of two electrons being released into the inner membrane which then react with with 2 hydrogen ion and a menaquinone to produce a menaquinol. This menaquinol then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before.
The third set of reactions starts with with formate interacting with a formate dehydrogenase-O resulting in a release of carbon dioxide and a hydrogen ion, this releases 2 electrons that interact with a menaquinone and two hydrogen ions. This releases a menaquinol which then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before
Metabolic
3
112379
Endocytosis
SubPathway
111969
41683
Compound
3518
8522521
Abaibou H, Pommier J, Benoit S, Giordano G, Mandrand-Berthelot MA: Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase. J Bacteriol. 1995 Dec;177(24):7141-9.
1653
Pathway
3519
9274019
Abaibou H, Giordano G, Mandrand-Berthelot MA: Suppression of Escherichia coli formate hydrogenlyase activity by trimethylamine N-oxide is due to drainage of the inducer formate. Microbiology. 1997 Aug;143 ( Pt 8):2657-64. doi: 10.1099/00221287-143-8-2657.
1653
Pathway
3520
17850256
Ansaldi M, Theraulaz L, Baraquet C, Panis G, Mejean V: Aerobic TMAO respiration in Escherichia coli. Mol Microbiol. 2007 Oct;66(2):484-94. doi: 10.1111/j.1365-2958.2007.05936.x. Epub 2007 Sep 10.
1653
Pathway
3521
3904597
Barrett EL, Kwan HS: Bacterial reduction of trimethylamine oxide. Annu Rev Microbiol. 1985;39:131-49. doi: 10.1146/annurev.mi.39.100185.001023.
1653
Pathway
3522
2168848
Berg BL, Stewart V: Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12. Genetics. 1990 Aug;125(4):691-702.
1653
Pathway
3523
7000002
Cox JC, Madigan MT, Favinger JL, Gest H: Redox mechanisms in "oxidant-dependent" hexose fermentation by Rhodopseudomonas capsulata. Arch Biochem Biophys. 1980 Oct 1;204(1):10-7.
1653
Pathway
3524
11004177
Gon S, Patte JC, Mejean V, Iobbi-Nivol C: The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli. J Bacteriol. 2000 Oct;182(20):5779-86.
1653
Pathway
3525
11884747
Jormakka M, Tornroth S, Byrne B, Iwata S: Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. doi: 10.1126/science.1068186.
1653
Pathway
3526
16221580
McCrindle SL, Kappler U, McEwan AG: Microbial dimethylsulfoxide and trimethylamine-N-oxide respiration. Adv Microb Physiol. 2005;50:147-98. doi: 10.1016/S0065-2911(05)50004-3.
1653
Pathway
3527
393699
Shimokawa O, Ishimoto M: Purification and some properties of inducible tertiary amine N-oxide reductase from Escherichia coli. J Biochem. 1979 Dec;86(6):1709-17.
1653
Pathway
3528
7031034
Takagi M, Tsuchiya T, Ishimoto M: Proton translocation coupled to trimethylamine N-oxide reduction in anaerobically grown Escherichia coli. J Bacteriol. 1981 Dec;148(3):762-8.
1653
Pathway
3529
12923080
Wang H, Gunsalus RP: Coordinate regulation of the Escherichia coli formate dehydrogenase fdnGHI and fdhF genes in response to nitrate, nitrite, and formate: roles for NarL and NarP. J Bacteriol. 2003 Sep;185(17):5076-85.
1653
Pathway
3530
2204318
Wissenbach U, Kroger A, Unden G: The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli. Arch Microbiol. 1990;154(1):60-6.
1653
Pathway
3531
1444716
Wissenbach U, Ternes D, Unden G: An Escherichia coli mutant containing only demethylmenaquinone, but no menaquinone: effects on fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate respiration. Arch Microbiol. 1992;158(1):68-73.
1653
Pathway
3533
6249272
Jones RW: The role of the membrane-bound hydrogenase in the energy-conserving oxidation of molecular hydrogen by Escherichia coli. Biochem J. 1980 May 15;188(2):345-50.
1653
Pathway
3534
11506918
Laurinavichene TV, Tsygankov AA: H2 consumption by Escherichia coli coupled via hydrogenase 1 or hydrogenase 2 to different terminal electron acceptors. FEMS Microbiol Lett. 2001 Aug 7;202(1):121-4.
1653
Pathway
3535
3905769
Sawers RG, Ballantine SP, Boxer DH: Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J Bacteriol. 1985 Dec;164(3):1324-31.
1653
Pathway
3536
18930017
Simon J, van Spanning RJ, Richardson DJ: The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems. Biochim Biophys Acta. 2008 Dec;1777(12):1480-90. doi: 10.1016/j.bbabio.2008.09.008. Epub 2008 Sep 30.
1653
Pathway
3537
9230919
Unden G, Bongaerts J: Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim Biophys Acta. 1997 Jul 4;1320(3):217-34.
1653
Pathway
3538
23260654
Volbeda A, Darnault C, Parkin A, Sargent F, Armstrong FA, Fontecilla-Camps JC: Crystal structure of the O(2)-tolerant membrane-bound hydrogenase 1 from Escherichia coli in complex with its cognate cytochrome b. Structure. 2013 Jan 8;21(1):184-190. doi: 10.1016/j.str.2012.11.010. Epub 2012 Dec 20.
1653
Pathway
3541
24715724
Wulff P, Day CC, Sargent F, Armstrong FA: How oxygen reacts with oxygen-tolerant respiratory [NiFe]-hydrogenases. Proc Natl Acad Sci U S A. 2014 May 6;111(18):6606-11. doi: 10.1073/pnas.1322393111. Epub 2014 Apr 8.
1653
Pathway
3542
363703
Yamamoto I, Ishimoto M: Hydrogen-dependent growth of Escherichia coli in anaerobic respiration and the presence of hydrogenases with different functions. J Biochem. 1978 Sep;84(3):673-9.
1653
Pathway
3545
8892824
Bogachev AV, Murtazina RA, Skulachev VP: H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells. J Bacteriol. 1996 Nov;178(21):6233-7.
1653
Pathway
3552
22392981
Wikstrom M, Hummer G: Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications. Proc Natl Acad Sci U S A. 2012 Mar 20;109(12):4431-6. doi: 10.1073/pnas.1120949109. Epub 2012 Mar 5.
1653
Pathway
1
Cell
CL:0000000
5
Hepatocyte
CL:0000182
4
Cardiomyocyte
CL:0000746
3
Neuron
CL:0000540
7
Epithelial Cell
CL:0000066
1
Homo sapiens
9606
Eukaryote
Human
2
Bacteria
2
Prokaryote
Bacteria
3
Escherichia coli
562
Prokaryote
12
Mus musculus
10090
Eukaryote
Mouse
5
Bos taurus
9913
Eukaryote
Cattle
17
Rattus norvegicus
10116
Eukaryote
Rat
19
Schizosaccharomyces pombe
4896
Eukaryote
24
Solanum lycopersicum
4081
Eukaryote
Tomato
4
Arabidopsis thaliana
3702
Eukaryote
Thale cress
18
Saccharomyces cerevisiae
4932
Eukaryote
Yeast
21
Xenopus laevis
8355
Eukaryote
African clawed frog
6
Caenorhabditis elegans
6239
Eukaryote
Roundworm
10
Drosophila melanogaster
7227
Eukaryote
Fruit fly
23
Pseudomonas aeruginosa
287
Prokaryote
60
Nitzschia sp.
0001
Eukaryote
Nitzschia4
25
Escherichia coli (strain K12)
83333
Prokaryote
49
Bathymodiolus platifrons
220390
Eukaryote
Deep sea mussel
3
Mitochondrial Matrix
GO:0005759
2
Mitochondrion
GO:0005739
5
Cytoplasm
GO:0005737
7
Endoplasmic Reticulum Membrane
GO:0005789
1
Cytosol
GO:0005829
4
Peroxisome
GO:0005777
12
Mitochondrial Inner Membrane
GO:0005743
6
Lysosome
GO:0005764
13
Endoplasmic Reticulum
GO:0005783
16
Lysosomal Lumen
GO:0043202
35
Chloroplast
GO:0009507
11
Extracellular Space
GO:0005615
14
Mitochondrial Outer Membrane
GO:0005741
24
Mitochondrial Intermembrane Space
GO:0005758
31
Periplasmic Space
GO:0005620
10
Cell Membrane
GO:0005886
36
Membrane
GO:0016020
53
Endoplasmic Reticulum Body
GO:0010168
34
Plant-Type Vacuole
GO:0000325
32
Inner Membrane
GO:0070258
25
Golgi apparatus
GO:0005794
18
Melanosome Membrane
GO:0033162
20
Endoplasmic Reticulum Lumen
GO:0005788
21
Synapse
GO:0045202
15
Nucleus
GO:0005634
40
Periplasm
GO:0042597
1
Liver
BTO:0000759
72
9
28
Stomach
BTO:0001307
155
26
8
Blood Vessel
BTO:0001102
74
11
4
Adrenal Medulla
BTO:0000049
71
8
25
Intestine
BTO:0000648
7
Nervous System
BTO:0001484
11
Heart
BTO:0000562
73
10
4
3
1
1
PW_BS000004
3
2
1
1
PW_BS000003
8
5
1
1
PW_BS000008
10
1
7
1
1
PW_BS000010
2
1
1
1
PW_BS000002
5
4
1
1
PW_BS000005
54
1
3
1
5
PW_BS000054
49
7
1
1
PW_BS000049
17
12
1
1
PW_BS000017
29
1
1
1
PW_BS000029
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6
1
1
PW_BS000009
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13
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1
PW_BS000018
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1
16
1
1
PW_BS000028
6
1
3
1
PW_BS000006
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1
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PW_BS000031
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1
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2
1
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3
3
1
PW_BS000103
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12
1
PW_BS000111
112
2
12
1
PW_BS000112
123
1
7
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1
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1
PW_BS000125
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1
PW_BS000135
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1
PW_BS000141
147
1
24
1
PW_BS000147
151
1
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1
PW_BS000151
155
3
24
1
PW_BS000155
161
3
18
1
PW_BS000161
1
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PW_BS000001
178
3
21
1
PW_BS000178
117
1
3
1
PW_BS000117
160
1
18
1
PW_BS000160
188
1
18
PW_BS000024
163
2
18
1
PW_BS000163
205
5
6
1
PW_BS000024
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2
6
1
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222
3
4
1
PW_BS000024
226
4
4
1
PW_BS000024
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35
4
1
PW_BS000024
224
2
4
1
PW_BS000024
198
5
18
1
PW_BS000024
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1
PW_BS000024
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13
4
1
PW_BS000024
298
1
7
10
1
PW_BS000024
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1
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1
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322
1
23
1
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PW_BS000132
133
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1
PW_BS000133
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PW_BS000028
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1
12
1
PW_BS000028
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1
PW_BS000028
130
13
12
1
PW_BS000130
113
6
12
1
PW_BS000113
347
1
3
12
5
PW_BS000028
368
3
60
1
PW_BS000028
119
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17
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PW_BS000119
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PW_BS000124
388
1
6
1
PW_BS000112
94
3
PW_BS000094
118
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PW_BS000118
406
3
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PW_BS000115
407
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425
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429
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PW_BS000115
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PW_BS000113
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PW_BS000115
481
2
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297
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299
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PW_BS000024
482
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495
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PW_BS000115
480
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PW_BS000115
501
3
6
1
PW_BS000115
502
4
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391
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PW_BS000112
395
13
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1
1
1
5
PW_BS000026
22
14
1
1
PW_BS000022
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24
1
1
PW_BS000042
70
28
5
1
1
PW_BS000070
107
31
3
PW_BS000107
105
11
3
PW_BS000105
157
2
24
1
PW_BS000157
159
24
PW_BS000159
166
1
1
PW_BS000166
152
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4
PW_BS000152
101
5
3
1
PW_BS000101
187
31
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PW_BS000024
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31
4
PW_BS000024
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1
4
PW_BS000024
213
7
18
1
PW_BS000024
210
13
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1
PW_BS000024
212
1
7
18
1
PW_BS000024
170
18
PW_BS000170
162
12
18
1
PW_BS000162
195
13
18
PW_BS000024
164
4
PW_BS000164
281
1
25
1
PW_BS000024
285
10
4
1
PW_BS000024
286
36
4
1
PW_BS000024
287
53
4
1
PW_BS000024
227
34
4
1
PW_BS000024
294
11
4
1
PW_BS000024
308
10
1
1
PW_BS000024
318
31
23
PW_BS000024
312
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PW_BS000024
320
11
23
PW_BS000024
293
4
1
PW_BS000024
114
11
12
PW_BS000114
327
1
1
12
5
PW_BS000028
345
24
12
1
PW_BS000028
310
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PW_BS000024
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2
PW_BS000024
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3
PW_BS000109
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PW_BS000115
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PW_BS000115
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PW_BS000137
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PW_BS000115
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PW_BS000115
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PW_BS000115
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PW_BS000115
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11
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PW_BS000024
506
24
6
1
PW_BS000115
317
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23
PW_BS000024
43
25
1
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PW_BS000043
356
25
12
1
PW_BS000028
419
25
5
1
PW_BS000115
455
25
17
1
PW_BS000115
490
25
10
1
PW_BS000115
507
25
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1
PW_BS000115
14
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PW_BS000014
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2
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PW_BS000013
20
4
1
1
1
PW_BS000020
33
18
1
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PW_BS000033
24
4
10
1
1
PW_BS000024
60
25
1
PW_BS000060
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PW_BS000046
72
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1
3
PW_BS000072
61
25
1
7
PW_BS000061
36
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20
1
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PW_BS000036
37
7
21
1
3
PW_BS000037
93
25
20
1
1
PW_BS000093
27
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PW_BS000027
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1
1
PW_BS000007
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1
5
2
1
PW_BS000097
110
2
3
1
PW_BS000110
127
1
16
5
1
PW_BS000127
129
1
5
12
1
PW_BS000129
140
10
3
PW_BS000140
143
1
5
19
1
PW_BS000143
146
5
19
1
PW_BS000146
180
2
21
1
PW_BS000180
207
6
6
1
PW_BS000024
211
10
18
PW_BS000024
214
25
18
1
PW_BS000024
215
6
18
1
PW_BS000024
190
11
18
PW_BS000024
277
1
2
18
PW_BS000024
65
11
1
PW_BS000065
290
5
49
1
PW_BS000024
291
6
49
1
PW_BS000024
292
4
49
1
PW_BS000024
301
6
10
1
PW_BS000024
302
1
16
10
1
PW_BS000024
253
5
4
1
PW_BS000024
333
1
2
12
PW_BS000028
115
10
12
PW_BS000115
337
1
16
12
1
PW_BS000028
341
4
1
12
1
PW_BS000028
343
18
12
1
PW_BS000028
329
14
12
1
PW_BS000028
352
25
12
PW_BS000028
353
25
12
7
PW_BS000028
360
4
10
12
1
PW_BS000028
370
2
60
1
PW_BS000028
228
36
1
PW_BS000024
232
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3
PW_BS000024
412
1
2
5
PW_BS000115
405
10
5
PW_BS000115
415
18
5
1
PW_BS000115
414
1
5
5
1
PW_BS000115
434
4
10
5
1
PW_BS000115
382
14
5
1
PW_BS000100
436
25
5
PW_BS000115
446
1
2
17
PW_BS000115
376
10
17
PW_BS000053
448
1
16
17
1
PW_BS000115
451
18
17
1
PW_BS000115
450
1
5
17
1
PW_BS000115
469
4
10
17
1
PW_BS000115
399
14
17
1
PW_BS000113
471
25
17
PW_BS000115
472
25
17
7
PW_BS000115
478
10
10
PW_BS000115
487
18
10
1
PW_BS000115
484
14
10
1
PW_BS000115
209
10
6
PW_BS000024
504
18
6
1
PW_BS000115
515
4
10
6
1
PW_BS000115
389
14
6
1
PW_BS000112
513
1
7
6
1
PW_BS000115
1144
NADH
HMDB0001487
NADH is the reduced form of NAD+, and NAD+ is the oxidized form of NADH, A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). It forms NADP with the addition of a phosphate group to the 2' position of the adenosyl nucleotide through an ester linkage.(Dorland, 27th ed).
58-68-4
C00004
439153
16908
NADH
388299
DB00157
NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](CO[P@](O)(=O)O[P@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N2C=NC3=C(N)N=CN=C23)[C@@H](O)[C@H]1O
C21H29N7O14P2
InChI=1S/C21H29N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1,3-4,7-8,10-11,13-16,20-21,29-32H,2,5-6H2,(H2,23,33)(H,34,35)(H,36,37)(H2,22,24,25)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
BOPGDPNILDQYTO-NNYOXOHSSA-N
[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]({[(2R,3S,4R,5R)-5-(3-carbamoyl-1,4-dihydropyridin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy})phosphinic acid
665.441
665.124771695
-2.35
8
NADH
0
-2
FDB022649
1,4-dihydronicotinamide adenine dinucleotide;Dpnh;Dihydrocodehydrogenase i;Dihydrocozymase;Dihydronicotinamide adenine dinucleotide;Dihydronicotinamide mononucleotide;Enada;Nadh;Nadh2;Reduced codehydrogenase i;Reduced diphosphopyridine nucleotide;Reduced nicotinamide adenine diphosphate;Reduced nicotinamide-adenine dinucleotide;B-dpnh;B-nadh;Beta-dpnh;Beta-nadh;Nicotinamide adenine dinucleotide (reduced);Reduced nicotinamide adenine dinucleotide
PW_C001144
NADH
143
4
153
3
490
8
648
10
1115
2
1275
5
1469
54
2230
49
2781
17
2836
29
3109
9
4806
18
4812
18
4821
28
4904
6
4959
31
5169
95
5240
103
5332
111
5358
112
5466
123
5479
125
5593
135
5698
100
5737
108
5829
141
5915
147
5945
151
6027
155
6079
161
6387
1
6472
178
6771
117
6893
160
7011
188
7099
163
7172
205
7195
206
7462
222
8244
226
8360
225
9086
224
11809
198
11821
216
12320
249
13003
298
13015
300
13255
223
42403
322
42618
315
77107
132
77123
133
77208
134
77371
331
77651
336
77668
334
77700
332
77707
130
77917
113
77986
347
80009
368
80691
119
93822
124
110549
388
112854
94
115838
118
119955
406
120172
407
120378
122
120986
408
121162
425
121244
126
121693
429
121818
383
122616
384
122745
120
123127
447
123138
136
123551
374
123734
460
123814
443
124242
464
124371
398
125189
121
125345
479
125531
481
125762
297
125808
299
125926
482
126516
495
126767
480
126888
501
127385
502
128090
390
128362
391
128429
395
40034
Hydrogen Ion
HMDB0059597
Hydrogen ion is recommended by IUPAC as a general term for all ions of hydrogen and its isotopes. Depending on the charge of the ion, two different classes can be distinguished: positively charged ions and negatively charged ions. Under aqueous conditions found in biochemistry, hydrogen ions exist as the hydrated form hydronium, H3O+, but these are often still referred to as hydrogen ions or even protons by biochemists. [WikiPedia])
C00080
1038
15378
1010
[H+]
H
InChI=1S/p+1
GPRLSGONYQIRFK-UHFFFAOYSA-N
hydron
1.0079
1.007825032
0
hydron
1
0
H+;H(+);Hydrogen cation;Hydron;Proton
PW_C040034
H+
215
4
670
8
753
15
788
31
848
3
1116
2
1463
26
1464
54
2231
49
2780
17
4250
22
4254
42
4547
10
4576
18
4694
70
5241
103
5327
111
5353
112
5626
108
5639
107
5699
100
5720
105
5742
117
5963
147
6037
155
6070
157
6093
161
6130
159
6232
166
6483
178
6601
152
6692
101
6843
188
6910
187
7100
163
7168
205
7191
206
7453
219
7454
220
7472
222
7525
213
7532
210
7558
212
7572
160
7590
170
8195
225
8218
151
8243
226
8413
162
8420
224
9139
195
9155
249
11915
164
12015
281
12181
285
12246
286
12266
287
12521
227
13257
223
13325
294
15330
308
42329
315
42354
318
42401
322
42405
312
42454
320
76912
293
77136
133
77210
134
77372
331
77804
114
77955
132
77990
327
77991
347
78379
345
79929
130
80019
368
80387
310
80388
304
80722
119
93823
124
94823
383
110550
388
112855
94
113280
390
115537
398
115539
118
115856
336
116205
109
119973
406
120193
407
120549
122
120593
409
121170
424
121171
425
122569
418
122615
384
122687
125
122758
120
123183
135
123218
137
123742
459
123743
460
125141
454
125188
121
125273
136
125359
479
125550
481
125730
483
125736
297
125809
299
126517
495
126717
489
126766
480
126823
300
126902
501
127213
208
128308
506
128361
391
128430
395
41683
menaquinone-8
Menaquinone 8, also known as vitamin MK 8 or MK-8, belongs to the class of organic compounds known as vitamin k compounds. These are quinone lipids containing a methylated naphthoquinone ring structure, and vary in the aliphatic side chain attached at the 3-position. Menaquinone 8 is considered to be a practically insoluble (in water) and relatively neutral molecule.
5376507
44027
[H]\C(CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC1=C(C)C(=O)C2=CC=CC=C2C1=O)=C(\C)CCC=C(C)C
C51H72O2
InChI=1S/C51H72O2/c1-38(2)20-13-21-39(3)22-14-23-40(4)24-15-25-41(5)26-16-27-42(6)28-17-29-43(7)30-18-31-44(8)32-19-33-45(9)36-37-47-46(10)50(52)48-34-11-12-35-49(48)51(47)53/h11-12,20,22,24,26,28,30,32,34-36H,13-19,21,23,25,27,29,31,33,37H2,1-10H3/b39-22+,40-24+,41-26+,42-28+,43-30+,44-32+,45-36+
LXKDFTDVRVLXFY-WQWYCSGDSA-N
2-methyl-3-[(2E,6E,10E,14E,18E,22E,26E)-3,7,11,15,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaen-1-yl]-1,4-dihydronaphthalene-1,4-dione
717.1162
716.553231548
-6.55
0
menaquinone-8
0
0
(all-e)-2-methyl-3-(3,7,11,15,19,23,27,31-octamethyl-2,6,10,14,18,22,26,30-dotriacontaoctaenyl)-1,4-naphthalenedione;2-methyl-3-[(2e,6e,10e,14e,18e,22e,26e)-3,7,11,15,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaen-1-yl]naphthalene-1,4-dione;2-methyl-3-[(2e,6e,10e,14e,18z,22e,26e)-3,7,11,15,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaen-1-yl]naphthalene-1,4-dione;Menaquinone 8;Menaquinone mk8;Menaquinone-8;Mk 8;Vitamin k2(40);Vitamin mk 8
PW_C041683
menaqn8
6625
109
43510
317
721
NAD
HMDB0000902
NAD (or Nicotinamide adenine dinucleotide) is used extensively in glycolysis and the citric acid cycle of cellular respiration. The reducing potential stored in NADH can be converted to ATP through the electron transport chain or used for anabolic metabolism. ATP "energy" is necessary for an organism to live. Green plants obtain ATP through photosynthesis, while other organisms obtain it by cellular respiration. (wikipedia). Nicotinamide adenine dinucleotide is a A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed).
53-84-9
C00003
5893
15846
NAD
5682
NC(=O)C1=C[N+](=CC=C1)[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N2C=NC3=C2N=CN=C3N)[C@@H](O)[C@H]1O
C21H28N7O14P2
InChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/p+1/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
BAWFJGJZGIEFAR-NNYOXOHSSA-O
1-[(2R,3R,4S,5R)-5-[({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)methyl]-3,4-dihydroxyoxolan-2-yl]-3-carbamoyl-1lambda5-pyridin-1-ylium
664.433
664.116946663
-2.59
8
1-[(2R,3R,4S,5R)-5-{[({[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxy]methyl}-3,4-dihydroxyoxolan-2-yl]-3-carbamoyl-1lambda5-pyridin-1-ylium
1
-1
FDB022309
3-carbamoyl-1-d-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate;3-carbamoyl-1-beta-d-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate inner salt;3-carbamoyl-1-beta-delta-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate inner salt;3-carbamoyl-1-delta-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate;Adenine-nicotinamide dinucleotide;Co-i;Codehydrase i;Codehydrogenase i;Coenzyme i;Cozymase;Cozymase i;Diphosphopyridine nucleotide;Diphosphopyridine nucleotide oxidized;Endopride;Nad trihydrate;Nad-oxidized;Nicotinamide adenine dinucleotide;Nicotinamide adenine dinucleotide oxidized;Nicotinamide dinucleotide;Nicotineamide adenine dinucleotide;Oxidized diphosphopyridine nucleotide;Pyridine nucleotide diphosphate;[(3s,2r,4r,5r)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl {[(3s,2r,4r,5r)-5-(3-carbamoylpyridyl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxyphosphoryl) hydrogen phosphate;[adenylate-32-p]-nad;Beta-diphosphopyridine nucleotide;Beta-nad;Beta-nicotinamide adenine dinucleotide;Beta-nicotinamide adenine dinucleotide trihydrate;Dpn;Nad;Nad+;Nadide;B-nad;β-nad
PW_C000721
NAD
140
4
150
3
353
8
651
10
1114
2
1134
43
1273
5
1466
54
2229
49
2779
17
2835
29
3107
9
4807
18
4813
18
4819
28
4902
6
4960
31
5167
95
5238
103
5334
111
5360
112
5469
123
5482
125
5590
135
5610
118
5696
100
5738
108
5827
141
5912
147
5942
151
6024
155
6072
157
6076
161
6385
1
6469
178
6772
117
6890
160
7012
188
7097
163
7174
205
7197
206
7405
198
7459
222
8241
226
8359
225
9085
224
11819
216
12322
249
13006
298
13018
300
13256
223
42404
322
42619
315
77104
132
77120
133
77209
134
77370
331
77650
336
77667
334
77702
332
77709
130
77915
113
77983
347
78406
356
80006
368
80690
119
93825
124
110552
388
112750
166
112853
94
119929
122
119952
406
120171
407
120834
419
120984
408
121159
425
121242
126
121259
429
121817
383
122614
384
122742
120
123130
447
123141
136
123419
455
123549
374
123731
460
123812
443
123829
464
124370
398
125187
121
125319
297
125342
479
125530
481
125806
299
125825
490
125924
482
126515
495
126765
480
126885
501
127278
507
127383
502
128089
390
128360
391
128428
395
41590
Menaquinol 8
Menaquinol 8, also known as mkh2-8, belongs to the class of organic compounds known as polyprenylphenols. Polyprenylphenols are compounds containing a polyisoprene chain attached to a phenol group. Menaquinol 8 is considered to be a practically insoluble (in water) and relatively neutral molecule. Menaquinol 8 may be a unique E.coli metabolite.
45479636
61684
[H]\C(CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC1=C(O)C2=CC=CC=C2C(O)=C1C)=C(\C)CCC=C(C)C
C51H74O2
InChI=1S/C51H74O2/c1-38(2)20-13-21-39(3)22-14-23-40(4)24-15-25-41(5)26-16-27-42(6)28-17-29-43(7)30-18-31-44(8)32-19-33-45(9)36-37-47-46(10)50(52)48-34-11-12-35-49(48)51(47)53/h11-12,20,22,24,26,28,30,32,34-36,52-53H,13-19,21,23,25,27,29,31,33,37H2,1-10H3/b39-22+,40-24+,41-26+,42-28+,43-30+,44-32+,45-36+
OIEZRVBFVPGODT-WQWYCSGDSA-N
2-methyl-3-[(2E,6E,10E,14E,18E,22E,26E)-3,7,11,15,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaen-1-yl]naphthalene-1,4-diol
719.1321
718.568881612
-6.49
2
menaquinol-8
0
0
Mkh2-8;Reduced menaquinone-8
PW_C041590
Menqol8
6626
109
43511
317
41100
Electron
An electron is a stable subatomic particle that is negatively charged. Electrons can be either free (not attached to any atom), or bound to atoms. Electrons exist in spherical shells of various radii representing energy levels. Electrons act as the primary carrier of electricity in solids.
PW_C041100
Electro
6627
108
6629
109
12840
225
13258
223
15252
249
43512
315
43520
317
77211
134
738
Trimethylamine N-oxide
HMDB0000925
Trimethylamine N-oxide (TMAO) is an oxidation product of trimethylamine and a common metabolite in animals and humans. In particular, trimethylamine-N-oxide is biosynthesized endogenously from trimethylamine, which is derived from choline, which can be derived from dietary lecithin (phosphatidylcholines) or dietary carnitine. TMAO decomposes to trimethylamine (TMA), which is the main odorant that is characteristic of degrading seafood. TMAO is an osmolyte that the body will use to counteract the effects of increased concentrations of urea (due to kidney failure) and high levels can be used as a biomarker for kidney problems. Fish odor syndrome or trimethylaminuria is a defect in the production of the enzyme flavin containing monooxygenase 3 (FMO3) causing incomplete breakdown of trimethylamine from choline-containing food into trimethylamine oxide. Trimethylamine then builds up and is released in the person's sweat, urine, and breath, giving off a strong fishy odor. The concentration of TMAO in the blood increases after consuming foods containing carnitine or lecithin (phosphatidylcholines), if the bacteria that convert those substances to TMAO are present in the gut (PMID: 23614584). High concentrations of carnitine are found in red meat, some energy drinks, and certain dietary supplements; lecithin is found in eggs and is commonly used as an ingredient in processed food. High levels of TMAO are found in many seafoods. Some types of normal gut bacteria (e.g. species of Acinetobacter) in the human gut convert dietary carnitine and dietary lecithin to TMAO (PMID: 21475195). TMAO alters cholesterol metabolism in the intestines, in the liver and in arterial wall. When TMAO is present, cholesterol metabolism is altered and there is an increased deposition of cholesterol within, and decreased removal of cholesterol from, peripheral cells such as those in the artery wall (PMID: 23563705).
1184-78-7
C01104
1145
15724
TRIMENTHLAMINE-N-O
1113
C[N+](C)(C)[O-]
C3H9NO
InChI=1S/C3H9NO/c1-4(2,3)5/h1-3H3
UYPYRKYUKCHHIB-UHFFFAOYSA-N
N,N-dimethylmethanamine oxide
75.1097
75.068413915
-0.11
0
trimethylamine-n-oxide
0
0
DBMET00513
FDB010413
N,n-dimethylmethanamine n-oxide;Tma-oxide;Tmao;Trimethylamine oxide;Trimethylamine-n-oxide;Triox;(ch3)3no;Me3n(+)o(-);Me3n(o);N(ch3)3o;Trimethylaminoxid;Trimethyloxamine
PW_C000738
TMAO
6628
107
43519
318
725
Trimethylamine
HMDB0000906
Trimethylamine, also known as NMe3, N(CH3)3, and TMA, is a colorless, hygroscopic, and flammable simple amine with a typical fishy odor in low concentrations and an ammonia like odor in higher concentrations. Trimethylamine has a boiling point of 2.9 degree centigrade and is a gas at room temperature. Trimethylamine usually comes in pressurized gas cylinders or as a 40% solution in water. Trimethylamine is a nitrogenous base and its positively charged cation is called trimethylammonium cation. A common salt of trimethylamine is trimethylammonium chloride, a hygroscopic colorless solid. -- Wikipedia; Trimethylamine is a product of decomposition of plants and animals. It is the substance mainly responsible for the fishy odor often associated with fouling fish, bacterial vagina infections, and bad breath. It is also associated with taking large doses of choline. -- Wikipedia; Trimethylaminuria is a genetic disorder in which the body is unable to metabolize trimethylamine from food sources. Patients develop a characteristic fish odour of their sweat, urine, and breath after the consumption of choline-rich foods. Trimethylaminuria is an autosomal recessive disorder involving a trimethylamine oxidase deficiency. Trimethylaminuria has also been observed in a certain breed of Rhode Island Red chicken that produces eggs with a fishy smell. -- Wikipedia.
75-50-3
C00565
1146
18139
TRIMENTHLAMINE-N-O
1114
CN(C)C
C3H9N
InChI=1S/C3H9N/c1-4(2)3/h1-3H3
GETQZCLCWQTVFV-UHFFFAOYSA-N
trimethylamine
59.1103
59.073499293
1.04
0
trimethylamine
0
1
FDB011944
Dimethylmethaneamine;N,n-dimethyl-methanamine;N-trimethylamine;Tma;Trimethylamine anhydrous;Trimethylamine aqueous solution;(ch3)3n;N(ch3)3;N,n,n-trimethylamine;Nme3;Tridimethylaminomethane;Trimethylamin
PW_C000725
TMA
6630
107
43521
318
1420
Water
HMDB0002111
Water is a chemical substance that is essential to all known forms of life. It appears colorless to the naked eye in small quantities, though it is actually slightly blue in color. It covers 71% of Earth's surface. Current estimates suggest that there are 1.4 billion cubic kilometers (330 million m3) of it available on Earth, and it exists in many forms. It appears mostly in the oceans (saltwater) and polar ice caps, but it is also present as clouds, rain water, rivers, freshwater aquifers, lakes, and sea ice. Water in these bodies perpetually moves through a cycle of evaporation, precipitation, and runoff to the sea. Clean water is essential to human life. In many parts of the world, it is in short supply. From a biological standpoint, water has many distinct properties that are critical for the proliferation of life that set it apart from other substances. It carries out this role by allowing organic compounds to react in ways that ultimately allow replication. All known forms of life depend on water. Water is vital both as a solvent in which many of the body's solutes dissolve and as an essential part of many metabolic processes within the body. Metabolism is the sum total of anabolism and catabolism. In anabolism, water is removed from molecules (through energy requiring enzymatic chemical reactions) in order to grow larger molecules (e.g. starches, triglycerides and proteins for storage of fuels and information). In catabolism, water is used to break bonds in order to generate smaller molecules (e.g. glucose, fatty acids and amino acids to be used for fuels for energy use or other purposes). Water is thus essential and central to these metabolic processes. Water is also central to photosynthesis and respiration. Photosynthetic cells use the sun's energy to split off water's hydrogen from oxygen. Hydrogen is combined with CO2 (absorbed from air or water) to form glucose and release oxygen. All living cells use such fuels and oxidize the hydrogen and carbon to capture the sun's energy and reform water and CO2 in the process (cellular respiration). Water is also central to acid-base neutrality and enzyme function. An acid, a hydrogen ion (H+, that is, a proton) donor, can be neutralized by a base, a proton acceptor such as hydroxide ion (OH-) to form water. Water is considered to be neutral, with a pH (the negative log of the hydrogen ion concentration) of 7. Acids have pH values less than 7 while bases have values greater than 7. Stomach acid (HCl) is useful to digestion. However, its corrosive effect on the esophagus during reflux can temporarily be neutralized by ingestion of a base such as aluminum hydroxide to produce the neutral molecules water and the salt aluminum chloride. Human biochemistry that involves enzymes usually performs optimally around a biologically neutral pH of 7.4. (Wikipedia).
7732-18-5
C00001
962
15377
937
O
H2O
InChI=1S/H2O/h1H2
XLYOFNOQVPJJNP-UHFFFAOYSA-N
water
18.0153
18.010564686
1
water
0
0
FDB013390
Dihydrogen oxide;Steam;[oh2];Acqua;Agua;Aqua;Bound water;Dihydridooxygen;Eau;H2o;Hoh;Hydrogen hydroxide;Wasser
PW_C001420
H2O
55
8
94
9
109
5
139
4
151
3
162
14
481
13
526
15
624
28
652
10
691
20
770
33
823
18
838
2
1094
31
1377
49
1465
54
1590
43
2018
24
2532
22
2678
60
2727
46
2778
17
2805
29
3143
70
3164
72
3634
61
4598
36
4727
37
4941
93
5030
27
5156
7
5195
97
5214
100
5227
94
5236
103
5297
105
5319
111
5343
113
5355
112
5402
110
5470
123
5483
125
5492
126
5507
127
5534
130
5537
114
5541
129
5591
135
5608
118
5622
108
5691
6
5759
140
5778
101
5841
143
5853
146
5877
107
5890
95
5910
147
5940
151
6032
155
6059
157
6087
161
6123
163
6133
159
6215
1
6218
166
6477
178
6507
180
6600
152
6713
117
6840
188
6888
160
7162
205
7181
207
7193
206
7211
211
7228
213
7238
214
7243
215
7295
198
7350
216
7388
210
7401
212
7467
222
7492
224
7500
190
7588
170
8201
225
8237
226
8414
162
9265
26
11850
277
11922
164
12011
281
12213
285
12250
286
12264
287
12327
249
12520
227
12632
65
12693
290
12705
291
12715
292
13007
298
13019
300
13025
301
13037
302
13261
223
13327
294
15340
308
42327
315
42695
318
43691
322
76914
293
77019
253
77102
132
77131
133
77215
134
77378
331
77397
332
77471
333
77516
115
77536
334
77628
336
77722
337
77759
341
77816
343
77982
347
78071
329
78235
352
78242
353
78270
356
79113
360
80014
368
80039
370
80591
228
80656
119
93830
383
94794
384
110557
390
110639
391
115844
398
119879
232
119915
122
119963
406
120008
407
120046
408
120113
124
120365
412
120430
405
120438
409
120606
415
120794
414
121158
425
121240
429
121351
121
121381
419
121607
434
122118
382
122384
436
122753
120
122797
374
122804
443
123012
446
123064
376
123072
137
123131
447
123142
136
123162
448
123231
451
123384
450
123730
460
123810
464
123940
455
124165
469
124670
399
124938
471
124945
472
125305
297
125353
479
125386
481
125424
482
125480
299
125682
483
125707
478
125745
487
126054
490
126238
495
126273
484
126764
480
126896
501
126963
502
127017
388
127177
208
127199
209
127227
504
127506
507
127576
515
127836
389
128082
395
128176
513
92
Formic acid
HMDB0000142
Formic acid is the simplest carboxylic acid. Formate is an intermediate in normal metabolism. It takes part in the metabolism of one-carbon compounds and its carbon may appear in methyl groups undergoing transmethylation. It is eventually oxidized to carbon dioxide. Formate is typically produced as a byproduct in the production of acetate. It is responsible for both metabolic acidosis and disrupting mitochondrial electron transport and energy production by inhibiting cytochrome oxidase activity, the terminal electron acceptor of the electron transport chain. Cell death from cytochrome oxidase inhibition by formate is believed to result partly from depletion of ATP, reducing energy concentrations so that essential cell functions cannot be maintained. Furthermore, inhibition of cytochrome oxidase by formate may also cause cell death by increased production of cytotoxic reactive oxygen species (ROS) secondary to the blockade of the electron transport chain. In nature, formic acid is found in the stings and bites of many insects of the order Hymenoptera, including bees and ants. The principal use of formic acid is as a preservative and antibacterial agent in livestock feed. When sprayed on fresh hay or other silage, it arrests certain decay processes and causes the feed to retain its nutritive value longer.
64-18-6
C00058
18971002
30751
FORMATE
278
DB01942
OC=O
CH2O2
InChI=1S/CH2O2/c2-1-3/h1H,(H,2,3)
BDAGIHXWWSANSR-UHFFFAOYSA-N
formic acid
46.0254
46.005479308
1.02
1
formic acid
0
-1
DBMET00489
FDB012804
Add-f;Ameisensaure;Aminate;Aminic acid;Bilorin;Collo-bueglatt;Collo-didax;Formate;Formira;Formisoton;Formylate;Formylic acid;Hydrogen carboxylate;Hydrogen carboxylic acid;Methanoate;Methanoic acid;Methanoic acid monomer;Myrmicyl;Sodium formate;Sybest;Wonderbond hardener m 600l
PW_C000092
Formate
946
8
977
3
1629
49
1943
2
5314
111
5348
112
6636
107
7158
205
7186
206
7325
213
7616
160
8287
210
11982
151
43522
318
76963
225
78652
132
78934
331
120670
122
120697
407
121496
383
121751
124
123284
135
123302
119
124054
398
124302
118
125753
297
125772
481
126478
299
126821
495
127637
388
128426
390
1316
Carbon dioxide
HMDB0001967
Carbon dioxide is a colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals. Carbon dioxide is produced during respiration by all animals, fungi and microorganisms that depend on living and decaying plants for food, either directly or indirectly. It is, therefore, a major component of the carbon cycle. Additionally, carbon dioxide is used by plants during photosynthesis to make sugars which may either be consumed again in respiration or used as the raw material to produce polysaccharides such as starch and cellulose, proteins and the wide variety of other organic compounds required for plant growth and development. When inhaled at concentrations much higher than usual atmospheric levels, it can produce a sour taste in the mouth and a stinging sensation in the nose and throat. These effects result from the gas dissolving in the mucous membranes and saliva, forming a weak solution of carbonic acid. Carbon dioxide is used by the food industry, the oil industry, and the chemical industry. Carbon dioxide is used to produce carbonated soft drinks and soda water. Traditionally, the carbonation in beer and sparkling wine comes about through natural fermentation, but some manufacturers carbonate these drinks artificially.
124-38-9
C00011
280
16526
274
O=C=O
CO2
InChI=1S/CO2/c2-1-3
CURLTUGMZLYLDI-UHFFFAOYSA-N
methanedione
44.0095
43.989829244
0.63
0
carbon dioxide
0
0
DBMET00423
FDB014084
Carbon oxide;Carbon-12 dioxide;Carbonic acid anhydride;Carbonic acid gas;Carbonic anhydride;[co2];Co2;E 290;E-290;E290;R-744
PW_C001316
CO2
50
8
121
1
204
4
480
13
503
18
640
3
677
31
695
20
806
5
1133
43
1638
49
1745
2
2551
17
3144
70
5283
103
5320
111
5750
108
5771
101
5968
100
6026
155
6078
161
6471
178
6637
107
6922
190
7017
160
7035
163
7061
188
7163
205
7308
198
7333
213
7461
222
7530
210
8215
225
8223
151
9158
249
11849
277
11908
170
12464
226
12688
290
42626
315
43523
318
76994
293
77122
133
77170
132
77470
333
77739
112
77750
129
77763
341
78077
134
78405
356
78427
334
78941
331
79227
130
80008
368
80675
119
80717
135
94836
384
113291
391
115549
121
119954
406
120089
122
120155
407
120364
412
120556
414
120833
419
120922
124
120991
408
121284
125
121505
383
122744
120
123011
446
123190
450
123418
455
123489
118
123556
374
123855
136
124063
398
125344
479
125460
297
125516
481
125824
490
125870
299
125931
482
126280
480
126887
501
127052
206
127277
507
127331
388
127390
502
6263
NADH-quinone oxidoreductase subunit A
P0AFC3
Involved in oxidoreductase activity, acting on NADH or NADPH. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoA
b2288
AP009048
3
1.6.99.5
6323
109
6266
NADH-quinone oxidoreductase subunit H
P0AFD4
Involved in oxidation-reduction process. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
nuoH
b2282
AP009048
3
1.6.99.5
6324
109
6268
NADH-quinone oxidoreductase subunit J
P0AFE0
Involved in NADH dehydrogenase (ubiquinone) activity. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoJ
b2280
AP009048
3
1.6.99.5
6325
109
6269
NADH-quinone oxidoreductase subunit K
P0AFE4
Involved in oxidoreductase activity, acting on NADH or NADPH. There are 2 NADH dehydrogenases in E.coli, however only this complex is able to use dNADH (reduced nicotinamide hypoxanthine dinucleotide, deamino-NADH) and dNADH-DB (dimethoxy- 5-methyl-6-decyl-1,4-benzoquinone) as substrates.
nuoK
b2279
AP009048
3
1.6.99.5
6326
109
6544
NADH-quinone oxidoreductase subunit L
P33607
Involved in NADH dehydrogenase (ubiquinone) activity. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoL
b2278
AP009048
3
1.6.99.5
6327
109
6270
NADH-quinone oxidoreductase subunit M
P0AFE8
Involved in NADH dehydrogenase (ubiquinone) activity. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoM
b2277
AP009048
3
1.6.99.5
6328
109
6271
NADH-quinone oxidoreductase subunit N
P0AFF0
Involved in NADH dehydrogenase (ubiquinone) activity. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoN
b2276
AP009048
3
1.6.99.5
6329
109
6265
NADH-quinone oxidoreductase subunit E
P0AFD1
Involved in oxidoreductase activity. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoE
b2285
AP009048
3
1.6.99.5
6330
109
6512
NADH-quinone oxidoreductase subunit F
P31979
Involved in NADH dehydrogenase (ubiquinone) activity. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoF
b2284
AP009048
3
1.6.99.5
6331
109
6543
NADH-quinone oxidoreductase subunit G
P33602
Involved in electron carrier activity. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoG
b2283
AP009048
3
1.6.99.5
6333
109
6264
NADH-quinone oxidoreductase subunit B
P0AFC7
Involved in NADH dehydrogenase (ubiquinone) activity. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoB
b2287
AP009048
3
1.6.99.5
6332
109
6542
NADH-quinone oxidoreductase subunit C/D
P33599
Involved in oxidoreductase activity, acting on NADH or NADPH. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoC
b2286
AP009048
3
1.6.99.5
6334
109
6267
NADH-quinone oxidoreductase subunit I
P0AFD6
Involved in electron carrier activity. NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
nuoI
b2281
AP009048
3
1.6.99.5
6335
109
7407
Cytochrome c-type protein torC
P33226
Involved in iron ion binding. Part of the anaerobic respiratory chain of trimethylamine-N-oxide reductase torA. Acts by transferring electrons from the membranous menaquinones to torA. This transfer probably involves an electron transfer pathway from menaquinones to the N-terminal domain of torC, then from the N-terminus to the C-terminus, and finally to torA. TorC apocytochrome negatively autoregulates the torCAD operon probably by inhibiting the torS kinase activity.
torC
b0996
AP009048
3
6631
109
7375
Trimethylamine-N-oxide reductase 1
P33225
Involved in oxidoreductase activity. Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.
torA
b0997
AP009048
3
1.7.2.3
6632
109
8861
232
6691
Hydrogenase-1 small chain
P69739
Involved in NADH dehydrogenase (ubiquinone) activity. This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth.
hyaA
b0972
AP009048
3
1.12.99.6
6633
109
135956
304
6212
Hydrogenase-1 large chain
P0ACD8
Involved in nickel cation binding. This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth.
hyaB
b0973
AP009048
3
1.12.99.6
6634
109
8866
140
135957
304
7282
Probable Ni/Fe-hydrogenase 1 B-type cytochrome subunit
P0AAM1
Involved in electron carrier activity. Probable b-type cytochrome.
hyaC
b0974
AP009048
3
6635
109
135958
304
6524
Formate dehydrogenase-O major subunit
P32176
Involved in formate dehydrogenase (NAD+) activity. Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site.
fdoG
b3894
AP009048
3
1.2.1.2
6638
109
6152
Formate dehydrogenase-O iron-sulfur subunit
P0AAJ5
Involved in electron carrier activity. Allows to use formate as major electron donor during aerobic respiration. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron- sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.
fdoH
b3893
AP009048
3
6639
109
6243
Formate dehydrogenase, cytochrome b556(fdo) subunit
P0AEL0
Involved in respiratory electron transport chain. Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase.
fdoI
b3892
AP009048
3
6640
109
3883
NADH:quinone oxidoreductase I
3
PW_P003883
10829
6263
10830
6266
10831
6268
10832
6269
10833
6544
10834
6270
10835
6271
10836
6265
10837
6512
10838
6543
10839
6264
10840
6542
10841
6267
3884
trimethylamine N-oxide reductase TorCA
3
PW_P003884
10842
7407
10843
7375
3885
hydrogenase 1, oxygen tolerant hydrogenase
3
PW_P003885
10844
6691
4
10845
6212
4
10846
7282
2
3886
formate dehydrogenase-O
3
PW_P003886
10847
6524
10848
6152
10849
6243
172
PW_RCT000172
Unknown
1020
172
1144
Compound
1
108
1021
172
40034
Compound
4
108
1022
172
40034
Compound
2
108
1023
172
41683
Compound
1
109
1024
172
721
Compound
1
108
1025
172
40034
Compound
1
108
1026
172
41590
Compound
1
109
1027
172
41100
Compound
1
108
1028
172
40034
Compound
4
108
172
173
PW_RCT000173
Right
1029
173
738
Compound
1
107
1030
173
40034
Compound
3
107
1031
173
41590
Compound
1
109
1032
173
41100
Compound
2
109
1033
173
725
Compound
1
107
1034
173
1420
Compound
1
107
1035
173
40034
Compound
2
107
1036
173
41683
Compound
1
109
173
174
PW_RCT000174
Right
1037
174
40034
Compound
1
107
1038
174
41100
Compound
1
109
1039
174
40034
Compound
2
108
1040
174
41683
Compound
1
109
1041
174
41590
Compound
1
109
1042
174
40034
Compound
1
107
174
175
PW_RCT000175
Right
1043
175
92
Compound
1
107
1044
175
41683
Compound
1
109
1045
175
41100
Compound
1
109
1046
175
40034
Compound
1
108
1047
175
1316
Compound
1
107
1048
175
40034
Compound
1
107
1049
175
41590
Compound
1
109
175
61475
1144
108
60
false
554
488
10
regular
50
30
61476
40034
108
55
false
930
608
10
regular
78
78
61477
40034
108
55
false
560
341
10
regular
78
78
61478
41683
109
3
false
319
399
10
regular
100
100
61479
721
108
59
false
1234
518
10
regular
50
30
61480
40034
108
55
false
925
233
10
regular
78
78
61481
41590
109
3
false
1504
406
10
regular
100
100
61482
41100
108
3
false
1334
306
10
regular
100
100
61483
40034
108
55
false
1315
501
10
regular
78
78
61484
738
107
3
false
1774
303
10
regular
100
110
61485
40034
107
55
false
1920
333
10
regular
78
78
61486
41100
109
3
false
1639
306
10
regular
100
100
61487
725
107
3
false
2424
296
10
regular
100
100
61488
1420
107
49
false
2320
316
10
regular
78
78
61489
40034
107
55
false
2160
259
10
regular
78
78
61490
41683
109
3
false
2519
402
10
regular
100
100
61491
40034
107
55
false
2653
928
10
regular
78
78
61492
41100
109
3
false
2621
782
10
regular
100
100
61493
40034
108
55
false
2381
938
10
regular
78
78
61494
41590
109
3
false
2526
1652
10
regular
100
100
61495
40034
107
55
false
2656
1293
10
regular
78
78
61496
738
107
3
false
2253
1762
10
regular
100
110
61497
40034
107
55
false
2143
1778
10
regular
78
78
61498
41100
109
3
false
2381
1767
10
regular
100
100
61499
725
107
3
false
1524
1772
10
regular
100
100
61500
1420
107
49
false
1654
1783
10
regular
78
78
61501
40034
107
55
false
1932
1808
10
regular
78
78
61502
41683
109
3
false
1380
1652
10
regular
100
100
61503
92
107
3
false
995
1754
10
regular
100
100
61504
41100
109
3
false
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1754
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100
61505
40034
108
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1764
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regular
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78
61506
1316
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52
false
511
1765
10
regular
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78
61507
40034
107
55
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1763
10
regular
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78
61508
41590
109
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1651
10
regular
100
100
61509
738
107
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false
222
1281
10
regular
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110
61510
40034
107
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false
237
1172
10
regular
78
78
61511
41100
109
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false
220
1431
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regular
100
100
61512
725
107
3
false
228
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10
regular
100
100
61513
1420
107
49
false
238
892
10
regular
78
78
61514
40034
107
55
false
171
1007
10
regular
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78
28638
6263
109
76
false
1014
418
10
subunit
regular
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70
28639
6266
109
76
false
669
473
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subunit
regular
150
70
28640
6268
109
76
false
669
363
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subunit
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70
28641
6269
109
76
false
779
363
8
subunit
regular
150
70
28642
6544
109
76
false
779
473
8
subunit
regular
150
70
28643
6270
109
76
false
1004
473
8
subunit
regular
150
70
28644
6271
109
76
false
1004
418
8
subunit
regular
150
70
28645
6265
109
76
false
1004
363
8
subunit
regular
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70
28646
6512
109
76
false
894
473
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subunit
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150
70
28647
6543
109
76
false
889
363
8
subunit
regular
150
70
28648
6264
109
76
false
894
418
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subunit
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150
70
28649
6542
109
76
false
779
418
8
subunit
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150
70
28650
6267
109
76
false
669
418
8
subunit
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70
28651
7407
109
76
false
2114
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8
subunit
regular
150
70
28652
7375
109
76
false
2049
419
8
subunit
regular
150
70
28653
6691
109
78
false
2505
1142
19
subunit
regular
135
120
28654
6212
109
78
false
2505
1022
20
subunit
regular
135
120
28655
7282
109
77
false
2485
1112
20
subunit
regular
160
80
28656
7407
109
76
false
1787
1669
8
subunit
regular
150
70
28657
7375
109
76
false
1897
1669
8
subunit
regular
150
70
28658
6524
109
76
false
600
1663
20
subunit
regular
150
70
28659
6152
109
76
false
725
1663
20
subunit
regular
150
70
28660
6243
109
76
false
845
1663
8
subunit
regular
150
70
948322
7407
109
76
false
296
1065
8
subunit
regular
150
70
948323
7375
109
76
false
296
1010
8
subunit
regular
150
70
24121
3883
1637
109
28326
28638
28327
28639
28328
28640
28329
28641
28330
28642
28331
28643
28332
28644
28333
28645
28334
28646
28335
28647
28336
28648
28337
28649
28338
28650
24122
3884
1637
109
28339
28651
28340
28652
24123
3885
1637
109
28341
28653
28342
28654
28343
28655
24124
3884
1637
109
28344
28656
28345
28657
24125
3886
1637
109
28346
28658
28347
28659
28348
28660
803136
3884
1637
109
944193
948322
944194
948323
88278
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5
false
18
88279
M969 608 C969 578 970 569 969 543
5
false
18
88280
M599 419 C601 451 639 453 669 453
5
false
18
88281
M419 449 C449 449 639 453 669 453
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false
18
88282
M1259 518 C1257 455 1223 455 1164 453
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18
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88283
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88288
M1959 411 C1961 459 2019 454 2049 454
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false
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88289
M1604 456 C1634 456 2019 454 2049 454
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false
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88290
M1689 406 C1692 465 2019 454 2049 454
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false
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88291
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88292
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false
88293
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88294
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false
88295
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false
18
88296
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false
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88297
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false
18
88298
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88299
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88300
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false
88301
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88302
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false
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88303
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false
18
88304
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88305
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88306
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88307
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88311
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88312
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88314
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3659819
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3659820
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3659821
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3659822
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18
3659823
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3659824
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3659825
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3659826
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