1861
Pathway
Nitrate Reduction VIII
NADH dehydrogenase and nitrate reductase can form the anaerobic respiratory chain that can be used for transferring electrons from NADH to nitrate with proton-motive force across cytoplasmic membrane. In E. coli K-12, NDH-I and NDH-II is the two energy conserving NADH dehydrogenases that do not contribute to proton gradient; but both of the enzymes are involved in anaerobic nitrate respiration. NDH-I might be acted as proton pump for translocating 4H+ per NADH oxidised (2e-). In E. coli K-12, there are also two energy conserving (H+/e- = 1) nitrate reductases (nitrate reductase A (NRA) and nitrate reductase Z (NRZ)). Nitrate reductase A can express under the condition of high levels of nitrate in environment; while the expression of nitrate reductase Z doesn't depend on nitrate levels or anaerobiosis. Nitrate and hydrogen atom will be catalyzed to form nitrite and water during nitrate reduction.
Metabolic
PW002092
Center
PathwayVisualizationContext2379
1804
1849
#000099
PathwayVisualization1845
1861
Nitrate Reduction VIII
NADH dehydrogenase and nitrate reductase can form the anaerobic respiratory chain that can be used for transferring electrons from NADH to nitrate with proton-motive force across cytoplasmic membrane. In E. coli K-12, NDH-I and NDH-II is the two energy conserving NADH dehydrogenases that do not contribute to proton gradient; but both of the enzymes are involved in anaerobic nitrate respiration. NDH-I might be acted as proton pump for translocating 4H+ per NADH oxidised (2e-). In E. coli K-12, there are also two energy conserving (H+/e- = 1) nitrate reductases (nitrate reductase A (NRA) and nitrate reductase Z (NRZ)). Nitrate reductase A can express under the condition of high levels of nitrate in environment; while the expression of nitrate reductase Z doesn't depend on nitrate levels or anaerobiosis. Nitrate and hydrogen atom will be catalyzed to form nitrite and water during nitrate reduction.
Metabolic
3
3926
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.
1861
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
3
Escherichia coli
562
Prokaryote
12
Mus musculus
10090
Eukaryote
Mouse
2
Bacteria
2
Prokaryote
Bacteria
24
Solanum lycopersicum
4081
Eukaryote
Tomato
18
Saccharomyces cerevisiae
4932
Eukaryote
Yeast
21
Xenopus laevis
8355
Eukaryote
African clawed frog
4
Arabidopsis thaliana
3702
Eukaryote
Thale cress
6
Caenorhabditis elegans
6239
Eukaryote
Roundworm
25
Escherichia coli (strain K12)
83333
Prokaryote
23
Pseudomonas aeruginosa
287
Prokaryote
60
Nitzschia sp.
0001
Eukaryote
Nitzschia4
17
Rattus norvegicus
10116
Eukaryote
Rat
5
Bos taurus
9913
Eukaryote
Cattle
10
Drosophila melanogaster
7227
Eukaryote
Fruit fly
19
Schizosaccharomyces pombe
4896
Eukaryote
49
Bathymodiolus platifrons
220390
Eukaryote
Deep sea mussel
3
Mitochondrial Matrix
GO:0005759
5
Cytoplasm
GO:0005737
11
Extracellular Space
GO:0005615
2
Mitochondrion
GO:0005739
1
Cytosol
GO:0005829
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
31
Periplasmic Space
GO:0005620
35
Chloroplast
GO:0009507
4
Peroxisome
GO:0005777
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
6
Lysosome
GO:0005764
16
Lysosomal Lumen
GO:0043202
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
8
5
1
1
PW_BS000008
15
11
1
PW_BS000015
31
1
5
1
1
PW_BS000031
3
2
1
1
PW_BS000003
2
1
1
1
PW_BS000002
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
111
5
12
1
PW_BS000111
112
2
12
1
PW_BS000112
108
1
3
PW_BS000108
107
31
3
PW_BS000107
100
5
2
1
PW_BS000100
105
11
3
PW_BS000105
117
1
3
1
PW_BS000117
147
1
24
1
PW_BS000147
155
3
24
1
PW_BS000155
157
2
24
1
PW_BS000157
161
3
18
1
PW_BS000161
159
24
PW_BS000159
166
1
1
PW_BS000166
178
3
21
1
PW_BS000178
152
8
4
PW_BS000152
101
5
3
1
PW_BS000101
188
1
18
PW_BS000024
187
31
18
PW_BS000024
163
2
18
1
PW_BS000163
205
5
6
1
PW_BS000024
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
160
1
18
1
PW_BS000160
170
18
PW_BS000170
225
35
4
1
PW_BS000024
151
1
4
1
PW_BS000151
226
4
4
1
PW_BS000024
162
12
18
1
PW_BS000162
224
2
4
1
PW_BS000024
195
13
18
PW_BS000024
249
13
4
1
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
223
12
4
1
PW_BS000024
294
11
4
1
PW_BS000024
308
10
1
1
PW_BS000024
315
1
23
PW_BS000024
318
31
23
PW_BS000024
322
1
23
1
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
132
1
12
1
PW_BS000132
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
124
1
5
1
PW_BS000124
383
7
5
1
PW_BS000100
388
1
6
1
PW_BS000112
94
3
PW_BS000094
390
7
6
1
PW_BS000112
398
7
17
1
PW_BS000113
118
1
17
1
PW_BS000118
336
1
12
1
PW_BS000028
109
32
3
PW_BS000109
406
3
5
1
PW_BS000115
407
2
5
1
PW_BS000115
122
5
5
1
PW_BS000122
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
135
5
17
1
PW_BS000135
137
11
17
PW_BS000137
459
1
1
17
5
PW_BS000115
460
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
297
5
10
1
PW_BS000024
299
1
10
1
PW_BS000024
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
29
1
1
1
PW_BS000029
9
6
1
1
PW_BS000009
28
1
16
1
1
PW_BS000028
6
1
3
1
PW_BS000006
95
1
7
2
1
PW_BS000095
123
1
7
5
1
PW_BS000123
141
1
7
19
1
PW_BS000141
1
1
PW_BS000001
198
5
18
1
PW_BS000024
216
4
18
1
PW_BS000024
298
1
7
10
1
PW_BS000024
334
4
12
1
PW_BS000028
332
1
7
12
1
PW_BS000028
113
6
12
1
PW_BS000113
408
4
5
1
PW_BS000115
126
6
5
1
PW_BS000126
429
1
5
1
PW_BS000115
447
1
7
17
1
PW_BS000115
374
4
17
1
PW_BS000053
443
6
17
1
PW_BS000115
464
1
17
1
PW_BS000115
482
4
10
1
PW_BS000115
502
4
6
1
PW_BS000115
43
25
1
1
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
6
1
PW_BS000115
14
10
1
PW_BS000014
13
1
2
1
PW_BS000013
20
4
1
1
1
PW_BS000020
33
18
1
1
PW_BS000033
24
4
10
1
1
PW_BS000024
60
25
1
PW_BS000060
46
1
1
4
PW_BS000046
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
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
40
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
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
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
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
1724
Nitrate
HMDB0002878
In inorganic chemistry, a nitrate is a salt of nitric acid. In organic chemistry the esters of nitric acid and various alcohols are called nitrates. The nitrate ion is a polyatomic anion with the empirical formula NO3- and a molecular mass of 62.01 daltons; it consists of one central nitrogen atom surrounded by three identical oxygen atoms in a trigonal planar arrangement. The nitrate ion carries a negative one formal charge. Nitrates should not be confused with nitrites, the salts of nitrous acid. Organic compounds containing the nitro functional group (which has the same formula and structure as the nitrate ion save that one of the O2 atoms is replaced by the R group) are known as nitro compounds. Nitrate ions can be toxic. In particular, nitrate toxicosis in humans occurs through enterohepatic metabolism of nitrates to ammonia, with nitrite being an intermediate. Nitrites oxidize the iron atoms in hemoglobin from Ferrous Iron (2+) to Ferric Iron (3+), rendering it unable to carry oxygen. This condition is called methemoglobinemia and can lead to a lack of oxygen in tissues. Methemoglobinemia can be treated with methylene blue. -- Wikipedia.
14797-55-8
C00244
943
17632
CPD-144
918
[O-][N+]([O-])=O
NO3
InChI=1S/NO3/c2-1(3)4/q-1
NHNBFGGVMKEFGY-UHFFFAOYSA-N
nitrate
62.0049
61.987817871
0
nitrate
-1
-1
FDB003811
Econazole nitrate;Femstat 3;Ganite;Gynazole-1;Isordil;Isosorbide dinitrate;Nitrate;Nitrate ion;Nitric acid;Sorbitrate;Trioxidonitrate;Trioxonitrate;[no3](-);Nitrate(1-);No3(-);Nitric acid ion;Nitric acid(1-)
PW_C001724
NO3
5222
94
6511
107
6512
108
6790
117
42314
315
42318
318
43759
322
1706
Nitrite
HMDB0002786
Nitrite is a nitrite compound is either a salt or an ester of nitrous acid. Sodium nitrite is used for the curing of meat because it prevents bacterial growth and, in a reaction with the meat's myoglobin, gives the product a desirable dark red color. Nitrite can be reduced to nitric oxide or ammonia by many species of bacteria. Under hypoxic conditions, nitrite may release nitric oxide, which causes potent vasodilation. Several mechanisms for nitrite conversion to NO have been described including enzymatic reduction by xanthine oxidoreductase, the mitochondria, and NO synthase (NOS), as well as nonenzymatic acidic disproportionation. -- Wikipedia.
14797-65-0
C00088
946
16301
NITRITE
921
ON=O
HNO2
InChI=1S/HNO2/c2-1-3/h(H,2,3)
IOVCWXUNBOPUCH-UHFFFAOYSA-N
nitrous acid
47.0134
47.000728281
1
nitrous acid
0
0
FDB023064
Nitrite;Nitrite anion;Nitrite ion;Nitrogen dioxide;Nitrogen dioxide ion;Nitrogen peroxide ion;[no2](-);Nitrit;Nitrite(1-);Nitrous acid, ion(1-);No2(-)
PW_C001706
NO2
6513
107
6514
108
6791
117
42319
318
42320
315
43760
322
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
217
"a menaquinone"
Compound
41380
Compound
PW_EC000217
AM
218
"a menaquinol"
Compound
41590
Compound
PW_EC000218
AM
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
5966
Respiratory nitrate reductase 1 alpha chain
P09152
Involved in oxidoreductase activity. The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.
narG
b1224
AP009048
3
1.7.99.4
6792
109
8533
140
113397
94
6308
Respiratory nitrate reductase 1 beta chain
P11349
Involved in iron-sulfur cluster binding. The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four 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.
narH
b1225
AP009048
3
1.7.99.4
6793
109
8534
140
113398
94
7523
Nitrate reductase molybdenum cofactor assembly chaperone NarJ
P0AF26
Involved in unfolded protein binding. Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with the NarI subunit on the membrane.
narJ
b1226
AP009048
3
6794
109
8535
101
113399
94
6309
Respiratory nitrate reductase 1 gamma chain
P11350
Involved in nitrate reductase activity. The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit.
narI
b1227
AP009048
3
1.7.99.4
6795
109
113400
94
6261
Respiratory nitrate reductase 2 gamma chain
P0AF32
Involved in nitrate reductase activity. This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit.
narV
b1465
AP009048
3
1.7.99.4
6796
109
113401
94
6377
Probable nitrate reductase molybdenum cofactor assembly chaperone NarW
P19317
Involved in unfolded protein binding. Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 2.
narW
b1466
AP009048
3
6797
109
8536
101
113402
94
6378
Respiratory nitrate reductase 2 beta chain
P19318
Involved in iron-sulfur cluster binding. This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four 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.
narY
b1467
AP009048
3
1.7.99.4
6798
109
8537
140
113403
94
6379
Respiratory nitrate reductase 2 alpha chain
P19319
Involved in oxidoreductase activity. The alpha chain is the actual site of nitrate reduction.
narZ
b1468
AP009048
3
1.7.99.4
6799
109
8538
140
113404
94
6547
Periplasmic nitrate reductase
P33937
Involved in oxidoreductase activity. Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein napC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism.
napA
b2206
AP009048
3
1.7.99.4
6800
109
8539
232
113405
94
7718
cytochrom c550 subunit nitrate reductase
P0ABL3
napB
3
6801
109
8540
232
113406
94
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
1166
Nitrate Reductase
3
PW_P001166
1339
5966
1340
6308
1341
7523
1342
6309
1343
6261
1344
6377
1345
6378
1346
6379
1347
6547
1348
7718
190
PW_RCT000190
Right
1131
190
40034
Compound
4
117
1132
190
1144
Compound
1
117
1133
190
40034
Compound
2
117
1134
190
217
ElementCollection
1
109
1135
190
40034
Compound
4
107
1136
190
721
Compound
1
117
1137
190
40034
Compound
1
117
1138
190
218
ElementCollection
1
109
190
191
PW_RCT000191
Right
1139
191
1724
Compound
1
117
1140
191
40034
Compound
2
117
1141
191
218
ElementCollection
1
109
1142
191
1706
Compound
1
117
1143
191
1420
Compound
1
117
1144
191
40034
Compound
2
107
1145
191
217
ElementCollection
1
109
191
71568
40034
117
55
false
539
453
10
regular
78
78
71569
1144
117
60
false
633
456
10
regular
50
30
71570
40034
117
55
false
439
456
10
regular
78
78
71571
40034
107
55
false
1254
255
10
regular
78
78
71572
721
117
59
false
1238
428
10
regular
50
30
71573
40034
117
55
false
1324
403
10
regular
78
78
71587
1724
117
3
false
1288
623
10
regular
100
100
71588
40034
117
55
false
1309
518
10
regular
78
78
71589
1706
117
3
false
1328
1176
10
regular
100
100
71590
1420
117
49
false
1339
1071
10
regular
78
78
71591
40034
107
55
false
1559
1089
10
regular
78
78
1515
217
37
109
false
363
318
12
regular
100
90
1516
218
37
109
false
1423
321
12
regular
100
90
1517
217
37
109
false
1433
1282
12
regular
100
90
32770
6263
109
76
false
703
338
8
subunit
regular
150
70
32771
6266
109
76
false
938
283
8
subunit
regular
150
70
32772
6268
109
76
false
703
388
8
subunit
regular
150
70
32773
6269
109
76
false
813
388
8
subunit
regular
150
70
32774
6544
109
76
false
923
388
8
subunit
regular
150
70
32775
6270
109
76
false
1028
388
8
subunit
regular
150
70
32776
6271
109
76
false
1053
388
8
subunit
regular
150
70
32777
6265
109
76
false
1038
338
8
subunit
regular
150
70
32778
6512
109
76
false
703
283
8
subunit
regular
150
70
32779
6543
109
76
false
818
283
8
subunit
regular
150
70
32780
6264
109
76
false
813
338
8
subunit
regular
150
70
32781
6542
109
76
false
923
338
8
subunit
regular
150
70
32782
6267
109
76
false
1048
283
8
subunit
regular
150
70
32790
5966
109
76
false
1403
737
8
subunit
regular
150
70
32791
6308
109
76
false
1338
787
8
subunit
regular
150
70
32792
7523
109
76
false
1453
787
8
subunit
regular
150
70
32793
6309
109
76
false
1338
837
8
subunit
regular
150
70
32794
6261
109
76
false
1453
837
8
subunit
regular
150
70
32795
6377
109
76
false
1338
882
8
subunit
regular
150
70
32796
6378
109
76
false
1453
882
8
subunit
regular
150
70
32797
6379
109
76
false
1333
927
8
subunit
regular
150
70
32798
6547
109
76
false
1453
932
8
subunit
regular
150
70
32799
7718
109
76
false
1408
982
8
subunit
regular
150
70
27535
3883
1845
109
32451
32770
32452
32771
32453
32772
32454
32773
32455
32774
32456
32775
32457
32776
32458
32777
32459
32778
32460
32779
32461
32780
32462
32781
32463
32782
27539
1166
1845
109
32471
32790
32472
32791
32473
32792
32474
32793
32475
32794
32476
32795
32477
32796
32478
32797
32479
32798
32480
32799
101587
M578 453 C578 398 637 375 703 373
5
false
18
101588
M478 456 C478 400 623 372 703 373
5
false
18
false
false
101589
M658 456 C659 398 673 373 703 373
5
false
18
false
false
101590
M1293 333 C1291 376 1268 372 1188 373
5
false
19
true
M 146.08198843774719 13.26155629629604 L 131.13513339358235 12 L 137.5160211147682 25.575134323078345
false
101591
M1263 428 C1264 367 1218 373 1188 373
5
false
18
true
M 146.08198843774719 13.26155629629604 L 131.13513339358235 12 L 137.5160211147682 25.575134323078345
false
101592
M1363 403 C1363 363 1282 373 1188 373
5
false
18
true
M 146.08198843774719 13.26155629629604 L 131.13513339358235 12 L 137.5160211147682 25.575134323078345
false
101593
M463 373 C514 374 604 372 703 373
5
false
18
101594
M1423 371 C1318 370 1292 373 1188 373
5
false
18
true
M 146.08198843774719 13.26155629629604 L 131.13513339358235 12 L 137.5160211147682 25.575134323078345
false
101611
M1388 673 C1418 673 1477 666 1478 737
5
false
18
101612
M1387 557 C1430 557 1476 614 1478 737
5
false
18
101613
M1428 1226 C1485 1226 1484 1120 1483 1052
5
false
18
true
M 162.59850474140725 863.1264100152231 L 147.65164969724242 861.8648537189271 L 154.03253741842826 875.4399880420054
false
101614
M1417 1110 C1455 1110 1483 1116 1483 1052
5
false
18
true
M 162.59850474140725 863.1264100152231 L 147.65164969724242 861.8648537189271 L 154.03253741842826 875.4399880420054
false
101615
M1559 1128 C1491 1128 1483 1115 1483 1052
5
false
18
true
M 162.59850474140725 863.1264100152231 L 147.65164969724242 861.8648537189271 L 154.03253741842826 875.4399880420054
false
101616
M1473 421 C1475 490 1478 686 1478 737
5
false
18
false
false
101617
M1483 1282 C1485 1219 1483 1179 1483 1052
5
false
18
true
M 162.59850474140725 863.1264100152231 L 147.65164969724242 861.8648537189271 L 154.03253741842826 875.4399880420054
false
448
190
1845
2498
71568
101587
Left
2499
71569
101588
Left
2500
71570
101589
Left
2501
71571
101590
Right
2502
71572
101591
Right
2503
71573
101592
Right
33
1515
101593
Left
34
1516
101594
Right
448
27535
224
449
191
1845
2504
71587
101611
Left
2505
71588
101612
Left
2506
71589
101613
Right
2507
71590
101614
Right
2508
71591
101615
Right
35
1516
101616
Left
36
1517
101617
Right
449
27539
225
186535
590
597
1.3
1.3
0
2
92
479
481
3600
M125 225 C125 175 175 125 225 125 C649 125 1200 125 1624 125 C1674 125 1724 175 1724 225 C1724 635 1724 1169 1724 1579 C1724 1629 1674 1679 1624 1679 C1200 1679 649 1679 225 1679 C175 1679 125 1629 125 1579 C125 1169 125 635 125 225
1
true
6
1599.0
1554.0
3601
M374 476 C374 426 424 376 474 376 C747 376 1102 376 1375 376 C1425 376 1475 426 1475 476 C1475 734 1475 1070 1475 1328 C1475 1378 1425 1428 1375 1428 C1102 1428 747 1428 474 1428 C424 1428 374 1378 374 1328 C374 1070 374 734 374 476
1
true
6
1101.0
1052.0