1884
Pathway
L-Cysteine Degradation
The degradation of cysteine starts with L-cysteine reacting with l-cysteine desulfhydrase resulting in the release of a hydrogen sulfide, a hydrogen ion and a a 2-aminoprop-2-enoate. The latter compound in turn reacts spontaneously to form a 2-iminopropanoate. This compound in turn reacts spontaneously with water and a hydrogen ion resulting in the release of ammonium and pyruvate.
Metabolic
PW002110
Center
PathwayVisualizationContext2397
1401
1350
#000099
PathwayVisualization1868
1884
L-Cysteine Degradation
The degradation of cysteine starts with L-cysteine reacting with l-cysteine desulfhydrase resulting in the release of a hydrogen sulfide, a hydrogen ion and a a 2-aminoprop-2-enoate. The latter compound in turn reacts spontaneously to form a 2-iminopropanoate. This compound in turn reacts spontaneously with water and a hydrogen ion resulting in the release of ammonium and pyruvate.
Metabolic
3
3986
12883870
Awano N, Wada M, Kohdoh A, Oikawa T, Takagi H, Nakamori S: Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli. Appl Microbiol Biotechnol. 2003 Aug;62(2-3):239-43. doi: 10.1007/s00253-003-1262-2. Epub 2003 Mar 20.
1884
Pathway
3987
16000837
Awano N, Wada M, Mori H, Nakamori S, Takagi H: Identification and functional analysis of Escherichia coli cysteine desulfhydrases. Appl Environ Microbiol. 2005 Jul;71(7):4149-52. doi: 10.1128/AEM.71.7.4149-4152.2005.
1884
Pathway
3988
704923
Cantarow WD, Cheung HT, Sundharadas G: Effects of prostaglandins on the spreading, adhesion and migration of mouse peritoneal macrophages. Prostaglandins. 1978 Jul;16(1):39-46.
1884
Pathway
3989
14907623
DELWICHE EA: Activators for the cysteine desulfhydrase system of an Escherichia coli mutant. J Bacteriol. 1951 Dec;62(6):717-22.
1884
Pathway
3990
7049234
Dwivedi CM, Ragin RC, Uren JR: Cloning, purification, and characterization of beta-cystathionase from Escherichia coli. Biochemistry. 1982 Jun 22;21(13):3064-9.
1884
Pathway
3991
13271322
METAXAS MA, DELWICHE EA: The L-cysteine desulfhydrase of Escherichia coli. J Bacteriol. 1955 Dec;70(6):735-7.
1884
Pathway
3992
9572924
Nakamori S, Kobayashi SI, Kobayashi C, Takagi H: Overproduction of L-cysteine and L-cystine by Escherichia coli strains with a genetically altered serine acetyltransferase. Appl Environ Microbiol. 1998 May;64(5):1607-11.
1884
Pathway
3993
14171448
NEWTON WA, SNELL EE: CATALYTIC PROPERTIES OF TRYPTOPHANASE, A MULTIFUNCTIONAL PYRIDOXAL PHOSPHATE ENZYME. Proc Natl Acad Sci U S A. 1964 Mar;51:382-9.
1884
Pathway
3994
1428472
Wang DY, De Stavola BL, Bulbrook RD, Allen DS, Kwa HG, Fentiman IS, Hayward JL, Millis RR: Relationship of blood prolactin levels and the risk of subsequent breast cancer. Int J Epidemiol. 1992 Apr;21(2):214-21.
1884
Pathway
3995
16820466
Yamada S, Awano N, Inubushi K, Maeda E, Nakamori S, Nishino K, Yamaguchi A, Takagi H: Effect of drug transporter genes on cysteine export and overproduction in Escherichia coli. Appl Environ Microbiol. 2006 Jul;72(7):4735-42. doi: 10.1128/AEM.02507-05.
1884
Pathway
1
Cell
CL:0000000
5
Hepatocyte
CL:0000182
4
Cardiomyocyte
CL:0000746
3
Neuron
CL:0000540
7
Epithelial Cell
CL:0000066
6
Myocyte
CL:0000187
1
Homo sapiens
9606
Eukaryote
Human
3
Escherichia coli
562
Prokaryote
18
Saccharomyces cerevisiae
4932
Eukaryote
Yeast
4
Arabidopsis thaliana
3702
Eukaryote
Thale cress
25
Escherichia coli (strain K12)
83333
Prokaryote
23
Pseudomonas aeruginosa
287
Prokaryote
12
Mus musculus
10090
Eukaryote
Mouse
17
Rattus norvegicus
10116
Eukaryote
Rat
5
Bos taurus
9913
Eukaryote
Cattle
10
Drosophila melanogaster
7227
Eukaryote
Fruit fly
6
Caenorhabditis elegans
6239
Eukaryote
Roundworm
2
Bacteria
2
Prokaryote
Bacteria
24
Solanum lycopersicum
4081
Eukaryote
Tomato
21
Xenopus laevis
8355
Eukaryote
African clawed frog
60
Nitzschia sp.
0001
Eukaryote
Nitzschia4
19
Schizosaccharomyces pombe
4896
Eukaryote
49
Bathymodiolus platifrons
220390
Eukaryote
Deep sea mussel
5
Cytoplasm
GO:0005737
1
Cytosol
GO:0005829
6
Lysosome
GO:0005764
11
Extracellular Space
GO:0005615
31
Periplasmic Space
GO:0005620
2
Mitochondrion
GO:0005739
34
Plant-Type Vacuole
GO:0000325
35
Chloroplast
GO:0009507
3
Mitochondrial Matrix
GO:0005759
7
Endoplasmic Reticulum Membrane
GO:0005789
12
Mitochondrial Inner Membrane
GO:0005743
14
Mitochondrial Outer Membrane
GO:0005741
24
Mitochondrial Intermembrane Space
GO:0005758
13
Endoplasmic Reticulum
GO:0005783
4
Peroxisome
GO:0005777
10
Cell Membrane
GO:0005886
36
Membrane
GO:0016020
53
Endoplasmic Reticulum Body
GO:0010168
32
Inner Membrane
GO:0070258
16
Lysosomal Lumen
GO:0043202
18
Melanosome Membrane
GO:0033162
25
Golgi apparatus
GO:0005794
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
9
Muscle
BTO:0000887
141
18
24
Brain
BTO:0000142
89
16
8
5
1
1
PW_BS000008
2
1
1
1
PW_BS000002
9
6
1
1
PW_BS000009
15
11
1
PW_BS000015
101
5
3
1
PW_BS000101
108
1
3
PW_BS000108
117
1
3
1
PW_BS000117
107
31
3
PW_BS000107
188
1
18
PW_BS000024
224
2
4
1
PW_BS000024
160
1
18
1
PW_BS000160
227
34
4
1
PW_BS000024
225
35
4
1
PW_BS000024
281
1
25
1
PW_BS000024
151
1
4
1
PW_BS000151
315
1
23
PW_BS000024
322
1
23
1
PW_BS000024
111
5
12
1
PW_BS000111
113
6
12
1
PW_BS000113
132
1
12
1
PW_BS000132
135
5
17
1
PW_BS000135
122
5
5
1
PW_BS000122
124
1
5
1
PW_BS000124
126
6
5
1
PW_BS000126
118
1
17
1
PW_BS000118
443
6
17
1
PW_BS000115
297
5
10
1
PW_BS000024
299
1
10
1
PW_BS000024
205
5
6
1
PW_BS000024
388
1
6
1
PW_BS000112
4
3
1
1
PW_BS000004
31
1
5
1
1
PW_BS000031
3
2
1
1
PW_BS000003
26
1
1
1
5
PW_BS000026
54
1
3
1
5
PW_BS000054
49
7
1
1
PW_BS000049
17
12
1
1
PW_BS000017
22
14
1
1
PW_BS000022
42
24
1
1
PW_BS000042
10
1
7
1
1
PW_BS000010
18
13
1
1
PW_BS000018
70
28
5
1
1
PW_BS000070
103
3
3
1
PW_BS000103
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2
12
1
PW_BS000112
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5
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11
3
PW_BS000105
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1
24
1
PW_BS000147
155
3
24
1
PW_BS000155
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2
24
1
PW_BS000157
161
3
18
1
PW_BS000161
159
24
PW_BS000159
166
1
1
PW_BS000166
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3
21
1
PW_BS000178
152
8
4
PW_BS000152
187
31
18
PW_BS000024
163
2
18
1
PW_BS000163
206
2
6
1
PW_BS000024
219
31
4
PW_BS000024
220
1
4
PW_BS000024
222
3
4
1
PW_BS000024
213
7
18
1
PW_BS000024
210
13
18
1
PW_BS000024
212
1
7
18
1
PW_BS000024
170
18
PW_BS000170
226
4
4
1
PW_BS000024
162
12
18
1
PW_BS000162
195
13
18
PW_BS000024
249
13
4
1
PW_BS000024
164
4
PW_BS000164
285
10
4
1
PW_BS000024
286
36
4
1
PW_BS000024
287
53
4
1
PW_BS000024
223
12
4
1
PW_BS000024
294
11
4
1
PW_BS000024
308
10
1
1
PW_BS000024
318
31
23
PW_BS000024
312
5
23
1
PW_BS000024
320
11
23
PW_BS000024
293
4
1
PW_BS000024
133
3
12
1
PW_BS000133
134
12
12
1
PW_BS000134
331
7
12
1
PW_BS000028
114
11
12
PW_BS000114
327
1
1
12
5
PW_BS000028
347
1
3
12
5
PW_BS000028
345
24
12
1
PW_BS000028
130
13
12
1
PW_BS000130
368
3
60
1
PW_BS000028
310
31
2
PW_BS000024
304
1
2
PW_BS000024
119
2
17
1
PW_BS000119
383
7
5
1
PW_BS000100
94
3
PW_BS000094
390
7
6
1
PW_BS000112
398
7
17
1
PW_BS000113
336
1
12
1
PW_BS000028
109
32
3
PW_BS000109
406
3
5
1
PW_BS000115
407
2
5
1
PW_BS000115
409
11
5
PW_BS000115
424
1
1
5
5
PW_BS000115
425
1
3
5
5
PW_BS000115
418
24
5
1
PW_BS000115
384
12
5
1
PW_BS000100
125
13
5
1
PW_BS000125
120
3
17
1
PW_BS000120
137
11
17
PW_BS000137
459
1
1
17
5
PW_BS000115
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1
3
17
5
PW_BS000115
454
24
17
1
PW_BS000115
121
12
17
1
PW_BS000121
136
13
17
1
PW_BS000136
479
3
10
1
PW_BS000115
481
2
10
1
PW_BS000115
483
11
10
PW_BS000115
495
7
10
1
PW_BS000115
489
24
10
1
PW_BS000115
480
12
10
1
PW_BS000115
300
13
10
1
PW_BS000024
501
3
6
1
PW_BS000115
208
11
6
PW_BS000024
506
24
6
1
PW_BS000115
391
12
6
1
PW_BS000112
395
13
6
1
PW_BS000113
5
4
1
1
PW_BS000005
14
10
1
PW_BS000014
13
1
2
1
PW_BS000013
28
1
16
1
1
PW_BS000028
20
4
1
1
1
PW_BS000020
33
18
1
1
PW_BS000033
43
25
1
1
PW_BS000043
24
4
10
1
1
PW_BS000024
60
25
1
PW_BS000060
46
1
1
4
PW_BS000046
29
1
1
1
PW_BS000029
72
5
1
3
PW_BS000072
61
25
1
7
PW_BS000061
36
1
20
1
1
PW_BS000036
37
7
21
1
3
PW_BS000037
93
25
20
1
1
PW_BS000093
27
15
1
PW_BS000027
7
1
1
PW_BS000007
97
1
5
2
1
PW_BS000097
110
2
3
1
PW_BS000110
123
1
7
5
1
PW_BS000123
127
1
16
5
1
PW_BS000127
129
1
5
12
1
PW_BS000129
6
1
3
1
PW_BS000006
140
10
3
PW_BS000140
143
1
5
19
1
PW_BS000143
146
5
19
1
PW_BS000146
95
1
7
2
1
PW_BS000095
1
1
PW_BS000001
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
198
5
18
1
PW_BS000024
216
4
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
298
1
7
10
1
PW_BS000024
301
6
10
1
PW_BS000024
302
1
16
10
1
PW_BS000024
253
5
4
1
PW_BS000024
332
1
7
12
1
PW_BS000028
333
1
2
12
PW_BS000028
115
10
12
PW_BS000115
334
4
12
1
PW_BS000028
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
356
25
12
1
PW_BS000028
360
4
10
12
1
PW_BS000028
370
2
60
1
PW_BS000028
228
36
1
PW_BS000024
232
40
3
PW_BS000024
408
4
5
1
PW_BS000115
412
1
2
5
PW_BS000115
405
10
5
PW_BS000115
415
18
5
1
PW_BS000115
414
1
5
5
1
PW_BS000115
429
1
5
1
PW_BS000115
419
25
5
1
PW_BS000115
434
4
10
5
1
PW_BS000115
382
14
5
1
PW_BS000100
436
25
5
PW_BS000115
374
4
17
1
PW_BS000053
446
1
2
17
PW_BS000115
376
10
17
PW_BS000053
447
1
7
17
1
PW_BS000115
448
1
16
17
1
PW_BS000115
451
18
17
1
PW_BS000115
450
1
5
17
1
PW_BS000115
464
1
17
1
PW_BS000115
455
25
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
482
4
10
1
PW_BS000115
478
10
10
PW_BS000115
487
18
10
1
PW_BS000115
490
25
10
1
PW_BS000115
484
14
10
1
PW_BS000115
502
4
6
1
PW_BS000115
209
10
6
PW_BS000024
504
18
6
1
PW_BS000115
507
25
6
1
PW_BS000115
515
4
10
6
1
PW_BS000115
389
14
6
1
PW_BS000112
513
1
7
6
1
PW_BS000115
50
9
5
1
6
PW_BS000050
156
12
24
1
PW_BS000156
177
1
21
1
PW_BS000177
85
24
10
1
1
PW_BS000085
346
9
5
12
6
PW_BS000028
367
1
60
1
PW_BS000028
423
9
5
5
6
PW_BS000115
458
9
5
17
6
PW_BS000115
448
L-Cysteine
HMDB0000574
Cysteine is a naturally occurring, sulfur-containing amino acid that is found in most proteins, although only in small quantities. Cysteine is unique amongst the twenty natural amino acids as it contains a thiol group. Thiol groups can undergo oxidation/reduction (redox) reactions; when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond. This reaction is reversible since the reduction of this disulphide bond regenerates two cysteine molecules. The disulphide bonds of cystine are crucial to defining the structures of many proteins. Cysteine is often involved in electron-transfer reactions, and help the enzyme catalyze its reaction. Cysteine is also part of the antioxidant glutathione. N-Acetyl-L-cysteine (NAC) is a form of cysteine where an acetyl group is attached to cysteine's nitrogen atom and is sold as a dietary supplement. Cysteine is named after cystine, which comes from the Greek word kustis meaning bladder (cystine was first isolated from kidney stones). Oxidation of cysteine can produce a disulfide bond with another thiol and further oxidation can produce sulphfinic or sulfonic acids. The cysteine thiol group is also a nucleophile and can undergo addition and substitution reactions. Thiol groups become much more reactive when they are ionized, and cysteine residues in proteins have pKa values close to neutrality, so they are often in their reactive thiolate form in the cell. The thiol group also has a high affinity for heavy metals and proteins containing cysteine will bind metals such as mercury, lead, and cadmium tightly. Due to this ability to undergo redox reactions, cysteine has antioxidant properties. Cysteine is an important source of sulfur in human metabolism, and although it is classified as a non-essential amino acid, cysteine may be essential for infants, the elderly, and individuals with certain metabolic disease or who suffer from malabsorption syndromes. Cysteine may at some point be recognized as an essential or conditionally essential amino acid (Wikipedia). Cysteine is important in energy metabolism. As cystine, it is a structural component of many tissues and hormones. Cysteine has clinical uses ranging from baldness to psoriasis to preventing smoker's hack. In some cases, oral cysteine therapy has proved excellent for treatment of asthmatics, enabling them to stop theophylline and other medications. Cysteine also enhances the effect of topically applied silver, tin, and zinc salts in preventing dental cavities. In the future, cysteine may play a role in the treatment of cobalt toxicity, diabetes, psychosis, cancer, and seizures (http://www.dcnutrition.com/AminoAcids/).
52-90-4
C00097
5862
17561
CYS
5653
DB00151
N[C@@H](CS)C(O)=O
C3H7NO2S
InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
XUJNEKJLAYXESH-REOHCLBHSA-N
(2R)-2-amino-3-sulfanylpropanoic acid
121.158
121.019749163
-0.72
3
L-cysteine
0
0
DBMET00503
FDB012678
(+)-2-amino-3-mercaptopropionic acid;(2r)-2-amino-3-mercaptopropanoate;(2r)-2-amino-3-mercaptopropanoic acid;(2r)-2-amino-3-sulfanylpropanoate;(2r)-2-amino-3-sulfanylpropanoic acid;(r)-(+)-cysteine;(r)-2-amino-3-mercaptopropanoate;(r)-2-amino-3-mercaptopropanoic acid;(r)-2-amino-3-mercapto-propanoate;(r)-2-amino-3-mercapto-propanoic acid;(r)-cysteine;2-amino-3-mercaptopropanoate;2-amino-3-mercaptopropanoic acid;2-amino-3-mercaptopropionate;2-amino-3-mercaptopropionic acid;3-mercapto-l-alanine;Acetylcysteine;B-mercaptoalanine;Carbocysteine;Cisteina;Cisteinum;Cystein;Cysteine;Cysteinum;Free cysteine;Half-cystine;L cysteine;L-(+)-cysteine;L-2-amino-3-mercaptopropanoate;L-2-amino-3-mercaptopropanoic acid;L-2-amino-3-mercaptopropionic acid;L-cystein;L-cysteine;Polycysteine;Thioserine;Alpha-amino-beta-thiolpropionic acid;Beta-mercaptoalanine;C;Cys;E920;L-zystein;(2r)-2-amino-3-sulphanylpropanoate;(2r)-2-amino-3-sulphanylpropanoic acid;L-2-amino-3-mercaptopropionate
PW_C000448
Cys
174
8
1867
2
2864
9
2870
15
5767
101
5801
108
6756
117
6759
107
7078
188
7496
224
7594
160
8256
227
8260
225
12012
281
12269
151
42651
315
43730
322
77778
111
77795
113
77796
132
80704
135
120125
122
120131
124
120580
126
122863
118
123210
443
125491
297
125498
299
127029
205
127035
388
1827
Hydrogen sulfide
HMDB0003276
Hydrogen sulfide is a highly toxic and flammable gas. Because it is heavier than air it tends to accumulate at the bottom of poorly ventilated spaces. Although very pungent at first, it quickly deadens the sense of smell, so potential victims may be unaware of its presence until it is too late. H2S arises from virtually anywhere where elemental sulfur comes into contact with organic material, especially at high temperatures. Hydrogen sulfide is a covalent hydride chemically related to water (H2O) since oxygen and sulfur occur in the same periodic table group. It often results when bacteria break down organic matter in the absence of oxygen, such as in swamps, and sewers (alongside the process of anaerobic digestion). It also occurs in volcanic gases, natural gas and some well waters. It is also important to note that Hydrogen sulfide is a central participant in the sulfur cycle, the biogeochemical cycle of sulfur on Earth. As mentioned above, sulfur-reducing and sulfate-reducing bacteria derive energy from oxidizing hydrogen or organic molecules in the absence of oxygen by reducing sulfur or sulfate to hydrogen sulfide. Other bacteria liberate hydrogen sulfide from sulfur-containing amino acids. Several groups of bacteria can use hydrogen sulfide as fuel, oxidizing it to elemental sulfur or to sulfate by using oxygen or nitrate as oxidant. The purple sulfur bacteria and the green sulfur bacteria use hydrogen sulfide as electron donor in photosynthesis, thereby producing elemental sulfur. (In fact, this mode of photosynthesis is older than the mode of cyanobacteria, algae and plants which uses water as electron donor and liberates oxygen).
7783-06-4
C00283
18779926
16136
HS
391
S
H2S
InChI=1S/H2S/h1H2
RWSOTUBLDIXVET-UHFFFAOYSA-N
hydrogen sulfide
34.081
33.987720754
1
hydrogen sulfide
0
-1
FDB009599
Acide sulfhydrique;Dihydrogen disulfide;Dihydrogen monosulfide;Dihydrogen sulfide;Hepatate;Hepatic acid;Hepatic gas;Hydrogen monosulfide;Hydrogen sulfide;Hydrogen-sulfide;Hydrogene sulfure;Hydrosulfurate;Hydrosulfuric acid;Idrogeno solforato;Schwefelwasserstoff;Sewer gas;Siarkowodor;Sour gas;Stink damp;Sulfur hydride;Sulfur hydroxide;Sulfureted hydrogen;Sulfuretted hydrogen;Zwavelwaterstof;[sh2];H2s;Hydrogen sulphide;Sulfide;Sulfure d'hydrogene;Acide sulphhydrique;Dihydrogen monosulphide;Dihydrogen sulphide;Hydrogen monosulphide;Hydrogen-sulphide;Hydrogene sulphure;Hydrosulfate;Hydrosulphate;Hydrosulphuric acid;Sulphide;Sulphure d'hydrogene
PW_C001827
H2SO
714
8
77785
111
120572
122
123206
135
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
40921
2-aminoprop-2-enoate
2-Aminoprop-2-enoate, also known as 2-aminoacrylate or 2,3-didehydroalaninate, belongs to the class of organic compounds known as alpha amino acids. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). 2-Aminoprop-2-enoate is soluble (in water) and a moderately acidic compound (based on its pKa). 2-Aminoprop-2-enoate may be a unique E.coli metabolite. 2-Aminoprop-2-enoate participates in a number of enzymatic reactions. In particular, Homocysteine and 2-aminoprop-2-enoate can be biosynthesized from L-cystathionine through the action of the enzymes bifunctional β-cystathionase, PLP-dependent and regulator OF maltose regulon and cystathionine-β-lyase / L-cysteine desulfhydrase. In addition, Hydrogen sulfide and 2-aminoprop-2-enoate can be biosynthesized from L-cysteine through the action of the enzyme tryptophanase / L-cysteine desulfhydrase.
58020
NC(=C)C([O-])=O
C3H4NO2
InChI=1S/C3H5NO2/c1-2(4)3(5)6/h1,4H2,(H,5,6)/p-1
UQBOJOOOTLPNST-UHFFFAOYSA-M
2-aminoprop-2-enoate
86.071
86.024751953
0.40
1
α-aminoacrylate
-1
0
PW_C040921
2A2E
8263
225
8365
151
40928
2-iminopropanoate
2-Iminopropanoate belongs to the class of organic compounds known as ketimines. These are organic compounds bearing the ketimine functional group, with the general structure R2C=NR' ( R is not a hydrogen ). 2-Iminopropanoate is slightly soluble (in water) and a weakly acidic compound (based on its pKa).
77456
CC(=N)C([O-])=O
C3H4NO2
InChI=1S/C3H5NO2/c1-2(4)3(5)6/h4H,1H3,(H,5,6)/p-1
DUAWRLXHCUAWMK-UHFFFAOYSA-M
2-iminopropanoate
86.071
86.024751953
-1.21
1
2-iminopropanoate
-1
0
PW_C040928
2-Isopa
8366
151
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
22608
Ammonium
HMDB0041827
Ammonium is an important source of nitrogen for many plant species, especially those growing on hypoxic soils. However, it is also toxic to most crop species and is rarely applied as a sole nitrogen source. The ammonium (more obscurely: aminium) cation is a positively charged polyatomic cation with the chemical formula NH4+. It is formed by the protonation of ammonia (NH3). Ammonium is also a general name for positively charged or protonated substituted amines and quaternary ammonium cations (NR4+), where one or more hydrogen atoms are replaced by organic radical groups (indicated by R).
14798-03-9
C01342
16741146
28938
218
[NH4+]
H4N
InChI=1S/H3N/h1H3/p+1
QGZKDVFQNNGYKY-UHFFFAOYSA-O
azanium
18.0385
18.034374133
1
azanium
1
1
Ammonium ion;Ammonia ion;Ammonium;Ammonium chloride;Ammonium(1+);Azanium;Nh4+;[nh4]+;[nh4](+);Nh4(+)
PW_C022608
Ammon
5751
108
5892
95
5969
100
6226
166
8273
151
8367
225
11909
170
12470
249
42627
315
116281
109
164
Pyruvic acid
HMDB0000243
Pyruvic acid is an intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed.) Biological Source: Intermediate in primary metabolism including fermentation processes. Present in muscle in redox equilibrium with Lactic acid. A common constituent, as a chiral cyclic acetal linked to saccharide residues, of bacterial polysaccharides. Isolated from cane sugar fermentation broth and peppermint. Constituent of Bauhinia purpurea, Cicer arietinum (chickpea), Delonix regia, Pisum sativum (pea) and Trigonella caerulea (sweet trefoil) Use/Importance: Reagent for regeneration of carbonyl compdounds from semicarbazones, phenylhydrazones and oximes. Flavoring ingredient (Dictionary of Organic Compounds).
127-17-3
C00022
1060
32816
PYRUVATE
1031
DB00119
CC(=O)C(O)=O
C3H4O3
InChI=1S/C3H4O3/c1-2(4)3(5)6/h1H3,(H,5,6)
LCTONWCANYUPML-UHFFFAOYSA-N
2-oxopropanoic acid
88.0621
88.016043994
0.18
1
pyruvic acid
0
-1
FDB008293
2-oxopropanoate;2-oxopropanoic acid;2-oxopropionate;2-oxopropionic acid;Acetylformate;Acetylformic acid;Bts;Pyroracemate;Pyroracemic acid;Pyruvate;A-ketopropionate;A-ketopropionic acid;Alpha-ketopropionate;Alpha-ketopropionic acid;2-ketopropionic acid;2-oxopropansaeure;2-oxopropionsaeure;Acide pyruvique;Alpha-oxopropionsaeure;Brenztraubensaeure;Ch3cocooh;2-ketopropionate;α-ketopropionate;α-ketopropionic acid;A-oxopropionsaeure;α-oxopropionsaeure
PW_C000164
Pyr
17
2
20
4
422
8
1181
3
1449
50
1457
26
5365
103
5405
117
5440
118
5444
120
5566
132
5570
133
5893
95
5920
147
5951
151
6022
155
6067
156
6074
161
6126
160
6383
1
6467
178
6510
177
6532
85
7457
222
7495
220
8200
225
12622
31
15292
249
15349
18
77310
111
77972
346
77978
327
78090
112
80004
368
80042
367
80695
135
112879
94
115683
121
119950
406
120011
124
120175
122
120878
407
121148
423
121154
424
123454
119
123720
458
123726
459
125340
479
125390
299
125534
297
125854
481
126883
501
126931
388
127067
205
127858
206
6070
Tryptophanase
P0A853
Involved in lyase activity. L-tryptophan + H(2)O = indole + pyruvate + NH(3).
tnaA
b3708
AP009048
3
4.1.99.1
8701
101
1513
tryptophanase / L-cysteine desulfhydrase
3
PW_P001513
1779
6070
4
6145
false
PW_R006145
Right
25148
448
1
Compound
false
25149
1827
1
Compound
false
25150
40034
1
Compound
false
25151
40921
1
Compound
false
6104
1513
6146
true
PW_R006146
Right
25152
40921
1
Compound
false
25153
40928
1
Compound
false
2903
true
PW_R002903
Right
11530
40928
1
Compound
false
11531
1420
1
Compound
false
11532
40034
1
Compound
false
11533
22608
1
Compound
false
11534
164
1
Compound
false
71785
448
3
false
304
416
10
regular
100
100
71786
1827
3
false
634
317
10
regular
100
110
71787
40034
55
false
660
542
10
regular
78
78
71788
40921
3
false
844
415
10
regular
100
110
71789
40928
3
false
844
605
10
regular
100
110
71790
1420
49
false
955
734
10
regular
78
78
71791
40034
55
false
750
732
10
regular
78
78
71792
22608
3
false
959
894
10
regular
100
100
71793
164
3
false
844
994
10
regular
100
100
32871
6070
101
8
false
474
428
8
subunit
regular
140
85
27603
1513
1868
32552
32871
101897
M404 466 C418 466 457 468 474 468
5
false
18
101898
M684 427 C685 472 644 468 614 468
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
101899
M699 542 C697 454 644 468 614 468
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
101900
M844 470 C814 470 644 468 614 468
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
101901
M939.3333333333335 470 C969.3333333333335 470 984.3333333333335 470 1014.3333333333335 470
5
true
18
101902
M894 605 C894 578 894 550 894 525
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
101903
M1134.3333333333335 850 C1164.3333333333335 850 1309.3333333333335 849 1339.3333333333335 849
5
true
18
101904
M955 773 C924 773 895.3333333333335 781 895.3333333333335 819
5
false
18
101905
M828 771 C875 772 894.3333333333335 792 895.3333333333335 828
5
false
18
101906
M959 944 C884 946 893.3333333333335 860 895.3333333333335 816
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
101907
M894 994 C893 966 897 736 894 715
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
20811
1868
6145
80843
71785
101897
Left
80844
71786
101898
Right
80845
71787
101899
Right
80846
71788
101900
Right
20980
6104
27603
20812
1868
6146
80847
71788
101901
Left
80848
71789
101902
Right
20813
1868
2903
80849
71789
101903
Left
80850
71790
101904
Left
80851
71791
101905
Left
80852
71792
101906
Right
80853
71793
101907
Right
186323
342
637
0.8
0.8
0
2
92
479
481
3645
M226 326 C226 276 276 226 326 226 C538 226 813 226 1025 226 C1075 226 1125 276 1125 326 C1125 553 1125 847 1125 1074 C1125 1124 1075 1174 1025 1174 C813 1174 538 1174 326 1174 C276 1174 226 1124 226 1074 C226 847 226 553 226 326
1
true
6
899.0
948.0
3646
M125 225 C125 175 175 125 225 125 C498 125 853 125 1126 125 C1176 125 1226 175 1226 225 C1226 513 1226 888 1226 1176 C1226 1226 1176 1276 1126 1276 C853 1276 498 1276 225 1276 C175 1276 125 1226 125 1176 C125 888 125 513 125 225
1
true
6
1101.0
1151.0