54
Pathway
Homocysteine Degradation
Homocysteine is an amino acid and homologue of cysteine that appears in the body as a result of the degradation of methionine. In mammals, homocysteine is used to biosynthesize cysteine via the following pathway. First the enzyme cystathionine beta-synthetase irreversibly condenses homocysteine with L-serine, forming L-cystathionine. The L-cystathionine is then cleaved by cystathionine gamma-lyase, producing 2-oxobutanoate, L-cysteine, and ammonia. The 2-oxobutanoate is further broken down via the 2-oxobutanoate degradation pathway, producing citric acid cycle intermediates, while the L-cysteine goes to the cysteine metabolism pathway. The homocysteine degradation pathway composes a part of the larger methionine metabolism pathway.
Metabolic
PW000027
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PathwayVisualizationContext27
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1300
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PathwayVisualization36
54
Homocysteine Degradation
Homocysteine is an amino acid and homologue of cysteine that appears in the body as a result of the degradation of methionine. In mammals, homocysteine is used to biosynthesize cysteine via the following pathway. First the enzyme cystathionine beta-synthetase irreversibly condenses homocysteine with L-serine, forming L-cystathionine. The L-cystathionine is then cleaved by cystathionine gamma-lyase, producing 2-oxobutanoate, L-cysteine, and ammonia. The 2-oxobutanoate is further broken down via the 2-oxobutanoate degradation pathway, producing citric acid cycle intermediates, while the L-cysteine goes to the cysteine metabolism pathway. The homocysteine degradation pathway composes a part of the larger methionine metabolism pathway.
Metabolic
1
246
102
SubPathway
370
590
Compound
8
247
19
SubPathway
371
590
Compound
8
248
98
SubPathway
372
120
Compound
8
249
349
SubPathway
373
3
Compound
8
250
68
SubPathway
374
448
Compound
8
251
27
SubPathway
375
448
Compound
8
252
62
SubPathway
376
448
Compound
8
1496
15539209
Finkelstein JD: Methionine metabolism in mammals. J Nutr Biochem. 1990 May;1(5):228-37.
54
Pathway
1497
3309559
Griffith OW: Mammalian sulfur amino acid metabolism: an overview. Methods Enzymol. 1987;143:366-76.
54
Pathway
1498
15189131
Stipanuk MH: Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine. Annu Rev Nutr. 2004;24:539-77. doi: 10.1146/annurev.nutr.24.012003.132418.
54
Pathway
1
Cell
CL:0000000
10
Glial cell
CL:0000125
3
Neuron
CL:0000540
5
Hepatocyte
CL:0000182
4
Cardiomyocyte
CL:0000746
7
Epithelial Cell
CL:0000066
6
Myocyte
CL:0000187
1
Homo sapiens
9606
Eukaryote
Human
17
Rattus norvegicus
10116
Eukaryote
Rat
4
Arabidopsis thaliana
3702
Eukaryote
Thale cress
12
Mus musculus
10090
Eukaryote
Mouse
5
Bos taurus
9913
Eukaryote
Cattle
10
Drosophila melanogaster
7227
Eukaryote
Fruit fly
6
Caenorhabditis elegans
6239
Eukaryote
Roundworm
3
Escherichia coli
562
Prokaryote
24
Solanum lycopersicum
4081
Eukaryote
Tomato
18
Saccharomyces cerevisiae
4932
Eukaryote
Yeast
23
Pseudomonas aeruginosa
287
Prokaryote
2
Bacteria
2
Prokaryote
Bacteria
19
Schizosaccharomyces pombe
4896
Eukaryote
21
Xenopus laevis
8355
Eukaryote
African clawed frog
25
Escherichia coli (strain K12)
83333
Prokaryote
49
Bathymodiolus platifrons
220390
Eukaryote
Deep sea mussel
60
Nitzschia sp.
0001
Eukaryote
Nitzschia4
5
Cytoplasm
GO:0005737
1
Cytosol
GO:0005829
35
Chloroplast
GO:0009507
3
Mitochondrial Matrix
GO:0005759
31
Periplasmic Space
GO:0005620
11
Extracellular Space
GO:0005615
2
Mitochondrion
GO:0005739
13
Endoplasmic Reticulum
GO:0005783
7
Endoplasmic Reticulum Membrane
GO:0005789
6
Lysosome
GO:0005764
4
Peroxisome
GO:0005777
10
Cell Membrane
GO:0005886
16
Lysosomal Lumen
GO:0043202
18
Melanosome Membrane
GO:0033162
25
Golgi Apparatus
GO:0005794
14
Mitochondrial Outer Membrane
GO:0005741
12
Mitochondrial Inner Membrane
GO:0005743
20
Endoplasmic Reticulum Lumen
GO:0005788
21
Synapse
GO:0045202
15
Nucleus
GO:0005634
36
Membrane
GO:0016020
53
Endoplasmic Reticulum Body
GO:0010168
34
Plant-Type Vacuole
GO:0000325
40
Periplasm
GO:0042597
24
Mitochondrial Intermembrane Space
GO:0005758
32
Inner Membrane
GO:0070258
7
Nervous System
BTO:0001484
1
Liver
BTO:0000759
72
9
4
Adrenal Medulla
BTO:0000049
71
8
25
Intestine
BTO:0000648
28
Stomach
BTO:0001307
155
26
8
Blood Vessel
BTO:0001102
74
11
11
Heart
BTO:0000562
73
10
6
Kidney
BTO:0000671
71
8
3
Sympathetic Nervous System
BTO:0001832
9
Muscle
BTO:0000887
141
18
24
Brain
BTO:0000142
89
16
8
5
1
1
PW_BS000008
2
1
1
1
PW_BS000002
135
5
17
1
PW_BS000135
225
35
4
1
PW_BS000024
111
5
12
1
PW_BS000111
132
1
12
1
PW_BS000132
122
5
5
1
PW_BS000122
124
1
5
1
PW_BS000124
118
1
17
1
PW_BS000118
297
5
10
1
PW_BS000024
299
1
10
1
PW_BS000024
205
5
6
1
PW_BS000024
388
1
6
1
PW_BS000112
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3
1
1
PW_BS000004
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31
3
PW_BS000107
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1
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PW_BS000108
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PW_BS000105
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1
24
1
PW_BS000147
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2
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PW_BS000163
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1
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PW_BS000024
202
7
11
1
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PW_BS000024
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11
1
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PW_BS000071
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1
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PW_BS000072
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1
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PW_BS000160
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PW_BS000003
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11
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PW_BS000015
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PW_BS000166
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PW_BS000024
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PW_BS000024
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PW_BS000151
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PW_BS000018
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PW_BS000049
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31
23
PW_BS000024
315
1
23
PW_BS000024
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3
12
1
PW_BS000133
331
7
12
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PW_BS000028
383
7
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PW_BS000100
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7
17
1
PW_BS000113
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3
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1
PW_BS000115
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3
17
1
PW_BS000120
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3
10
1
PW_BS000115
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PW_BS000115
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PW_BS000005
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PW_BS000014
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PW_BS000028
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PW_BS000010
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PW_BS000020
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18
1
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PW_BS000033
31
1
5
1
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PW_BS000031
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1
3
1
5
PW_BS000054
43
25
1
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PW_BS000043
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4
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1
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PW_BS000024
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PW_BS000022
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PW_BS000060
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PW_BS000017
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PW_BS000112
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PW_BS000123
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PW_BS000125
126
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PW_BS000126
127
1
16
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PW_BS000127
130
13
12
1
PW_BS000130
114
11
12
PW_BS000114
129
1
5
12
1
PW_BS000129
6
1
3
1
PW_BS000006
140
10
3
PW_BS000140
101
5
3
1
PW_BS000101
143
1
5
19
1
PW_BS000143
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PW_BS000146
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1
7
2
1
PW_BS000095
155
3
24
1
PW_BS000155
157
2
24
1
PW_BS000157
161
3
18
1
PW_BS000161
159
24
PW_BS000159
1
1
PW_BS000001
178
3
21
1
PW_BS000178
180
2
21
1
PW_BS000180
152
8
4
PW_BS000152
117
1
3
1
PW_BS000117
188
1
18
PW_BS000024
207
6
6
1
PW_BS000024
206
2
6
1
PW_BS000024
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10
18
PW_BS000024
213
7
18
1
PW_BS000024
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18
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PW_BS000024
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6
18
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PW_BS000024
198
5
18
1
PW_BS000024
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PW_BS000024
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13
18
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PW_BS000024
212
1
7
18
1
PW_BS000024
222
3
4
1
PW_BS000024
190
11
18
PW_BS000024
170
18
PW_BS000170
226
4
4
1
PW_BS000024
162
12
18
1
PW_BS000162
26
1
1
1
5
PW_BS000026
277
1
2
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
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
300
13
10
1
PW_BS000024
301
6
10
1
PW_BS000024
302
1
16
10
1
PW_BS000024
223
12
4
1
PW_BS000024
294
11
4
1
PW_BS000024
308
10
1
1
PW_BS000024
322
1
23
1
PW_BS000024
293
4
1
PW_BS000024
253
5
4
1
PW_BS000024
134
12
12
1
PW_BS000134
332
1
7
12
1
PW_BS000028
333
1
2
12
PW_BS000028
115
10
12
PW_BS000115
334
4
12
1
PW_BS000028
336
1
12
1
PW_BS000028
337
1
16
12
1
PW_BS000028
341
4
1
12
1
PW_BS000028
343
18
12
1
PW_BS000028
347
1
3
12
5
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
368
3
60
1
PW_BS000028
370
2
60
1
PW_BS000028
228
36
1
PW_BS000024
119
2
17
1
PW_BS000119
384
12
5
1
PW_BS000100
390
7
6
1
PW_BS000112
391
12
6
1
PW_BS000112
232
40
3
PW_BS000024
407
2
5
1
PW_BS000115
408
4
5
1
PW_BS000115
412
1
2
5
PW_BS000115
405
10
5
PW_BS000115
409
11
5
PW_BS000115
415
18
5
1
PW_BS000115
414
1
5
5
1
PW_BS000115
425
1
3
5
5
PW_BS000115
429
1
5
1
PW_BS000115
121
12
17
1
PW_BS000121
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
443
6
17
1
PW_BS000115
446
1
2
17
PW_BS000115
376
10
17
PW_BS000053
137
11
17
PW_BS000137
447
1
7
17
1
PW_BS000115
136
13
17
1
PW_BS000136
448
1
16
17
1
PW_BS000115
451
18
17
1
PW_BS000115
450
1
5
17
1
PW_BS000115
460
1
3
17
5
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
481
2
10
1
PW_BS000115
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4
10
1
PW_BS000115
483
11
10
PW_BS000115
478
10
10
PW_BS000115
487
18
10
1
PW_BS000115
490
25
10
1
PW_BS000115
495
7
10
1
PW_BS000115
484
14
10
1
PW_BS000115
480
12
10
1
PW_BS000115
502
4
6
1
PW_BS000115
208
11
6
PW_BS000024
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
395
13
6
1
PW_BS000113
513
1
7
6
1
PW_BS000115
790
6
11
1
PW_BS000524
834
6
1
1
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PW_BS000549
185
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19
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418
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17
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PW_BS000115
458
9
5
17
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17
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489
24
10
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PW_BS000115
506
24
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PW_BS000115
109
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PW_BS000109
590
Homocysteine
HMDB0000742
Homocysteine is a sulfur-containing amino acid that arises during methionine metabolism. Although its concentration in plasma is only about 10 micromolar (uM), even moderate hyperhomocysteinemia is associated with increased incidence of cardiovascular disease and Alzheimer's disease. Elevations in plasma homocysteine are commonly found as a result of vitamin deficiencies, polymorphisms of enzymes of methionine metabolism, and renal disease. Pyridoxal, folic acid, riboflavin, and Vitamin B(12) are all required for methionine metabolism, and deficiency of each of these vitamins result in elevated plasma homocysteine. A polymorphism of methylenetetrahydrofolate reductase (C677T), which is quite common in most populations with a homozygosity rate of 10-15 %, is associated with moderate hyperhomocysteinemia, especially in the context of marginal folate intake. Plasma homocysteine is inversely related to plasma creatinine in patients with renal disease. This is due to an impairment in homocysteine removal in renal disease. The role of these factors, and of modifiable lifestyle factors, in affecting methionine metabolism and in determining plasma homocysteine levels is discussed. Homocysteine is an independent cardiovascular disease (CVD) risk factor modifiable by nutrition and possibly exercise. Homocysteine was first identified as an important biological compound in 1932 and linked with human disease in 1962 when elevated urinary homocysteine levels were found in children with mental retardation. This condition, called homocysteinuria, was later associated with premature occlusive CVD, even in children. These observations led to research investigating the relationship of elevated homocysteine levels and CVD in a wide variety of populations including middle age and elderly men and women with and without traditional risk factors for CVD. (PMID 17136938, 15630149).
454-29-5
C05330
49791978
17230
HOMO-CYS
757
N[C@@H](CCS)C(O)=O
C4H9NO2S
InChI=1S/C4H9NO2S/c5-3(1-2-8)4(6)7/h3,8H,1-2,5H2,(H,6,7)/t3-/m0/s1
FFFHZYDWPBMWHY-VKHMYHEASA-N
(2S)-2-amino-4-sulfanylbutanoic acid
135.185
135.035399227
-0.96
3
L-homocysteine
0
0
DBMET00508
FDB001491
(+-)-homocysteine;(s)-2-amino-4-mercapto-butanoate;(s)-2-amino-4-mercapto-butanoic acid;2-amino-4-mercapto-butanoate;2-amino-4-mercapto-butanoic acid;2-amino-4-mercapto-butyric acid;2-amino-4-mercapto-dl-butyrate;2-amino-4-mercapto-dl-butyric acid;2-amino-4-mercaptobutyric acid;2-amino-4-sulfanylbutanoate;2-amino-4-sulfanylbutanoic acid;D,l-homocysteine;Dl-2-amino-4-mercaptobutyric acid;Dl-2-amino-4-mercapto-butyric acid;Dl-homocysteine;Dl-homocysteine (free base);Hcy;Homo-cys;Homocysteine;L-2-amino-4-mercapto-butyric acid;L-homocysteine;Usaf b-12;2-amino-4-mercaptobutyrate
PW_C000590
Hcys
566
8
1824
2
5595
135
8264
225
77607
111
78105
132
120476
122
122151
124
124703
118
125793
297
126310
299
127248
205
127872
388
120
L-Serine
HMDB0000187
Serine is a nonessential amino acid derived from glycine. Like all the amino acid building blocks of protein and peptides, serine can become essential under certain conditions, and is thus important in maintaining health and preventing disease. Low-average concentration of serine compared to other amino acids is found in muscle. Serine is highly concentrated in all cell membranes. (http://www.dcnutrition.com/AminoAcids/) L-Serine may be derived from four possible sources: dietary intake; biosynthesis from the glycolytic intermediate 3-phosphoglycerate; from glycine ; and by protein and phospholipid degradation. Little data is available on the relative contributions of each of these four sources of l-serine to serine homoeostasis. It is very likely that the predominant source of l-serine will be very different in different tissues and during different stages of human development. In the biosynthetic pathway, the glycolytic intermediate 3-phosphoglycerate is converted into phosphohydroxypyruvate, in a reaction catalyzed by 3-phosphoglycerate dehydrogenase (3- PGDH; EC 1.1.1.95). Phosphohydroxypyruvate is metabolized to phosphoserine by phosphohydroxypyruvate aminotransferase (EC 2.6.1.52) and, finally, phosphoserine is converted into l-serine by phosphoserine phosphatase (PSP; EC 3.1.3.3). In liver tissue, the serine biosynthetic pathway is regulated in response to dietary and hormonal changes. Of the three synthetic enzymes, the properties of 3-PGDH and PSP are the best documented. Hormonal factors such as glucagon and corticosteroids also influence 3-PGDH and PSP activities in interactions dependent upon the diet. L-serine plays a central role in cellular proliferation. L-Serine is the predominant source of one-carbon groups for the de novo synthesis of purine nucleotides and deoxythymidine monophosphate. It has long been recognized that, in cell cultures, L-serine is a conditional essential amino acid, because it cannot be synthesized in sufficient quantities to meet the cellular demands for its utilization. In recent years, L-serine and the products of its metabolism have been recognized not only to be essential for cell proliferation, but also to be necessary for specific functions in the central nervous system. The findings of altered levels of serine and glycine in patients with psychiatric disorders and the severe neurological abnormalities in patients with defects of L-serine synthesis underscore the importance of L-serine in brain development and function. (PMID 12534373).
56-45-1
C00065
5951
17115
SER
5736
DB00133
N[C@@H](CO)C(O)=O
C3H7NO3
InChI=1S/C3H7NO3/c4-2(1-5)3(6)7/h2,5H,1,4H2,(H,6,7)/t2-/m0/s1
MTCFGRXMJLQNBG-REOHCLBHSA-N
(2S)-2-amino-3-hydroxypropanoic acid
105.0926
105.042593095
0.66
3
L-serine
0
0
FDB012739
(-)-serine;(s)-2-amino-3-hydroxypropanoate;(s)-2-amino-3-hydroxypropanoic acid;(s)-2-amino-3-hydroxy-propanoate;(s)-2-amino-3-hydroxy-propanoic acid;(s)-serine;(s)-a-amino-b-hydroxypropionate;(s)-a-amino-b-hydroxypropionic acid;(s)-alpha-amino-beta-hydroxypropionate;(s)-alpha-amino-beta-hydroxypropionic acid;(s)-b-amino-3-hydroxypropionate;(s)-b-amino-3-hydroxypropionic acid;(s)-beta-amino-3-hydroxypropionate;(s)-beta-amino-3-hydroxypropionic acid;2-amino-3-hydroxypropanoate;2-amino-3-hydroxypropanoic acid;3-hydroxy-l-alanine;L-(-)-serine;L-3-hydroxy-2-aminopropionate;L-3-hydroxy-2-aminopropionic acid;L-3-hydroxy-alanine;L-ser;Serine;B-hydroxy-l-alanine;Beta-hydroxy-l-alanine;Beta-hydroxyalanine;(2s)-2-amino-3-hydroxypropanoic acid;(s)-(-)-serine;L-2-amino-3-hydroxypropionic acid;L-serin;S;Ser;(2s)-2-amino-3-hydroxypropanoate;(s)-α-amino-β-hydroxypropionate;(s)-α-amino-β-hydroxypropionic acid;β-hydroxy-l-alanine;B-hydroxyalanine;β-hydroxyalanine;L-2-amino-3-hydroxypropionate
PW_C000120
Ser
344
8
1810
2
2617
4
5642
107
5643
108
5884
105
6011
147
6907
163
7086
201
7087
202
7090
71
7091
72
7202
160
7438
3
7443
15
7444
166
7522
224
8357
225
9154
249
12173
151
12625
18
15379
49
42335
318
42336
315
77320
111
78088
133
78112
132
79979
331
94858
383
115752
398
119924
122
122056
124
122136
406
122718
135
124667
118
124688
120
125314
297
126209
299
126293
479
126860
205
127771
388
127856
501
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
140674
790
140675
834
140755
185
67
L-Cystathionine
HMDB0000099
Cystathionine is a dipeptide formed by serine and homocysteine. Cystathioninuria is a prominent manifestation of vitamin-B6 deficiency. The transsulfuration of methionine yields homocysteine, which combines with serine to form cystathionine, the proximate precursor of cysteine through the enzymatic activity of cystathionase. In conditions in which cystathionine gamma-synthase or cystathionase is deficient, for example, there is cystathioninuria. Although cystathionine has not been detected in normal human serum or plasma by most conventional methods, gas chromatographic/mass spectrometric methodology detected a mean concentration of cystathionine in normal human serum of 140 nM, with a range of 65 to 301 nM.567 Cystathionine concentrations in CSF have been 10, 1, and 0.5 uM, and "not detected." Only traces (i.e., <1 uM) of cystathionine are present in normal CSF.587. gamma-Cystathionase deficiency provided the first instance in which, in a human, the major biochemical abnormality due to a defined enzyme defect was clearly shown to be alleviated by administration of large doses of pyridoxine. The response in gamma-cystathionase-deficient patients is not attributable to correction of a preexisting deficiency of this vitamin. (OMMBID, Chap. 88).
56-88-2
C02291
25243997
17482
L-CYSTATHIONINE
388392
N[C@@H](CCSC[C@H](N)C(O)=O)C(O)=O
C7H14N2O4S
InChI=1S/C7H14N2O4S/c8-4(6(10)11)1-2-14-3-5(9)7(12)13/h4-5H,1-3,8-9H2,(H,10,11)(H,12,13)/t4-,5-/m0/s1
ILRYLPWNYFXEMH-WHFBIAKZSA-N
(2S)-2-amino-4-{[(2R)-2-amino-2-carboxyethyl]sulfanyl}butanoic acid
222.262
222.067427636
-1.11
4
L-cystathionine
0
0
DBMET00486
FDB001976
(r)-s-(2-amino-2-carboxyethyl)-l-homocysteine;Cystathionine;L-(+)-cystathionine;S-[(2r)-2-amino-2-carboxyethyl]-l-homocysteine;[r-(r*,s*)]-2-amino-4-[(2-amino-2-carboxyethyl)thio]-butanoate;[r-(r*,s*)]-2-amino-4-[(2-amino-2-carboxyethyl)thio]-butanoic acid;S-(beta-amino-beta-carboxyethyl)homocysteine
PW_C000067
L-Cystt
1048
8
1828
2
8257
227
8261
225
78125
132
78162
111
120761
122
122174
124
123358
135
124726
118
125794
297
126331
299
127249
205
127894
388
1148
Pyridoxal 5'-phosphate
HMDB0001491
This is the active form of vitamin B6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (pyridoxamine). -- Pubchem; Pyridoxal-phosphate (PLP, pyridoxal-5'-phosphate) is a cofactor of many enzymatic reactions. It is the active form of vitamin B6 which comprises three natural organic compounds, pyridoxal, pyridoxamine and pyridoxine. -- Wikipedia.
54-47-7
C00018
1051
18405
PYRIDOXAL_PHOSPHATE
1022
DB00114
CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O
C8H10NO6P
InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
NGVDGCNFYWLIFO-UHFFFAOYSA-N
[(4-formyl-5-hydroxy-6-methylpyridin-3-yl)methoxy]phosphonic acid
247.1419
247.024573569
-1.64
3
pyridoxal phosphate
0
-2
FDB021820
Apolon b6;Biosechs;Codecarboxylase;Coenzyme b6;Hairoxal;Hexermin-p;Hi-pyridoxin;Hiadelon;Himitan;Pal-p;Plp;Phosphopyridoxal;Phosphopyridoxal coenzyme;Pidopidon;Piodel;Pydoxal;Pyridoxal 5'-phosphate;Pyridoxal 5-phosphate;Pyridoxal p;Pyridoxal phosphate;Pyridoxal-p;Pyridoxyl phosphate;Pyromijin;Sechvitan;Vitahexin-p;Vitazechs;3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinecarboxaldehyde;3-hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde 5-phosphate;Phosphoric acid mono-(4-formyl-5-hydroxy-6-methyl-pyridin-3-ylmethyl) ester;Pyridoxal 5-monophosphoric acid ester;Pyridoxal 5'-(dihydrogen phosphate);Pyridoxal-5'-phosphate;Pyridoxal 5'-phosphoric acid;3-hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde 5-phosphoric acid;Phosphate mono-(4-formyl-5-hydroxy-6-methyl-pyridin-3-ylmethyl) ester;Pyridoxal 5-monophosphate ester;Pyridoxal 5'-(dihydrogen phosphoric acid);Pyridoxal 5-phosphoric acid;Pyridoxal phosphoric acid;Pyridoxal-5'-phosphoric acid
PW_C001148
Pyr-5'P
18
2
32
4
45
3
51
8
122
1
401
19
696
20
1110
42
1450
50
1458
26
2120
10
2150
49
5325
111
5416
117
5421
103
5441
118
5455
120
5567
132
5581
133
6533
85
7018
160
7167
205
7216
212
7222
213
11858
161
12175
151
12623
31
12628
18
12684
289
12689
290
77017
253
77037
225
77041
293
77052
224
77526
112
77764
341
77973
346
77979
327
78292
345
78855
332
78862
331
80696
135
98630
7
119912
122
120024
124
120029
406
120087
407
120817
418
121149
423
121155
424
122069
123
122076
383
122834
119
123402
454
123721
458
123727
459
124620
447
124627
398
125302
297
125402
299
125407
479
125458
481
125803
489
126224
298
126231
495
126942
388
126947
501
126996
206
127258
506
127786
513
127793
390
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
3
2-Ketobutyric acid
HMDB0000005
2-Ketobutyric acid is a substance that is involved in the metabolism of many amino acids (glycine, methionine, valine, leucine, serine, threonine, isoleucine) as well as propanoate metabolism and C-5 branched dibasic acid metabolism. More specifically, alpha-ketobutyric acid is a product of the lysis of cystathionine. It is also one of the degradation products of threonine. It can be converted into propionyl-CoA (and subsequently methylmalonyl CoA, which can be converted into succinyl CoA, a citric acid cycle intermediate), and thus enter the citric acid cycle.
600-18-0
C00109
58
30831
2-OXOBUTANOATE
57
DB04553
CCC(=O)C(O)=O
C4H6O3
InChI=1S/C4H6O3/c1-2-3(5)4(6)7/h2H2,1H3,(H,6,7)
TYEYBOSBBBHJIV-UHFFFAOYSA-N
2-oxobutanoic acid
102.0886
102.031694058
-0.11
1
2-oxobutanoic acid
0
-1
FDB003359
2-ketobutanoate;2-ketobutanoic acid;2-ketobutyrate;2-oxo-butanoate;2-oxo-butanoic acid;2-oxo-butyrate;2-oxo-butyric acid;2-oxo-n-butyrate;2-oxo-n-butyric acid;2-oxobutanoate;2-oxobutanoic acid;2-oxobutyrate;2-oxobutyric acid;3-methylpyruvate;3-methylpyruvic acid;Methyl-pyruvate;Methyl-pyruvic acid;Propionyl-formate;Propionyl-formic acid;A-keto-n-butyrate;A-keto-n-butyric acid;A-ketobutyrate;A-ketobutyric acid;A-oxo-n-butyrate;A-oxo-n-butyric acid;A-oxobutyrate;A-oxobutyric acid;Alpha-keto-n-butyrate;Alpha-keto-n-butyric acid;Alpha-ketobutric acid;Alpha-ketobutyrate;Alpha-ketobutyric acid;Alpha-oxo-n-butyrate;Alpha-oxo-n-butyric acid;Alpha-oxobutyrate;Alpha-oxobutyric acid;2-ketobutyric acid;3-methyl pyruvic acid;3-methyl pyruvate;α-ketobutyrate;α-ketobutyric acid;α-oxo-n-butyrate;α-oxo-n-butyric acid
PW_C000003
2KBA
337
8
1868
2
2692
3
8274
151
8383
225
42272
4
78126
132
78163
111
78643
133
79027
112
119922
122
122176
124
122274
406
122577
407
122716
135
124728
118
124829
120
125149
119
125312
297
126333
299
126438
479
126726
481
126858
205
127896
388
128007
501
128319
206
35
Ammonia
HMDB0000051
Ammonia is a colourless alkaline gas and is one of the most abundant nitrogen-containing compounds in the atmosphere. It is an irritant with a characteristic pungent odor that is widely used in industry. Inasmuch as ammonia is highly soluble in water and, upon inhalation, is deposited in the upper airways, occupational exposures to ammonia have commonly been associated with sinusitis, upper airway irritation, and eye irritation. Acute exposures to high levels of ammonia have also been associated with diseases of the lower airways and interstitial lung. Small amounts of ammonia are naturally formed in nearly all tissues and organs of the vertebrate organism. Ammonia is both a neurotoxin and a metabotoxin. In fact, it is the most common endogenous neurotoxin. A neurotoxin is a compound that causes damage to neural tissue and neural cells. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. Ammonia is recognized to be central in the pathogenesis of a brain condition known as hepatic encephalopathy, which arises from various liver diseases and leads to a build up ammonia in the blood (hyperammonemia). More than 40% of people with cirrhosis develop hepatic encephalopathy. Part of the neurotoxicity of ammonia arises from the fact that it easily crosses the blood-brain barrier and is absorbed and metabolized by the astrocytes, a population of cells in the brain that constitutes 30% of the cerebral cortex. Astrocytes use ammonia when synthesizing glutamine from glutamate. The increased levels of glutamine lead to an increase in osmotic pressure in the astrocytes, which become swollen. There is increased activity of the inhibitory gamma-aminobutyric acid (GABA) system, and the energy supply to other brain cells is decreased. This can be thought of as an example of brain edema. The source of the ammonia leading to hepatic encephalopathy is not entirely clear. The gut produces ammonia, which is metabolized in the liver, and almost all organ systems are involved in ammonia metabolism. Colonic bacteria produce ammonia by splitting urea and other amino acids, however this does not fully explain hyperammonemia and hepatic encephalopathy. The alternative explanation is that hyperammonemia is the result of the intestinal breakdown of amino acids, especially glutamine. The intestines have significant glutaminase activity, predominantly located in the enterocytes. On the other hand, intestinal tissues only have a little glutamine synthetase activity, making it a major glutamine-consuming organ. In addition to the intestine, the kidney is an important source of blood ammonia in patients with liver disease. Ammonia is also taken up by the muscle and brain in hepatic coma, and there is confirmation that ammonia is metabolized in muscle. Excessive formation of ammonia in the brains of Alzheimer's disease patients has also been demonstrated, and it has been shown that some Alzheimer's disease patients exhibit elevated blood ammonia concentrations. Ammonia is the most important natural modulator of lysosomal protein processing. Indeed, there is strong evidence for the involvement of aberrant lysosomal processing of beta-amyloid precursor protein (beta-APP) in the formation of amyloid deposits. Inflammatory processes and activation of microglia are widely believed to be implicated in the pathology of Alzheimer's disease. Ammonia is able to affect the characteristic functions of microglia, such as endocytosis, and cytokine production. Based on these facts, an ammonia-based hypothesis for Alzheimer's disease has been suggested (PMID: 17006913, 16167195, 15377862, 15369278). Chronically high levels of ammonia in the blood are associated with nearly twenty different inborn errors of metabolism including: 3-hydroxy-3-methylglutaryl-CoA lyase deficiency, 3-methyl-crotonylglycinuria, argininemia, argininosuccinic aciduria, beta-ketothiolase deficiency, biotinidase deficiency, carbamoyl phosphate synthetase deficiency, carnitine-acylcarnitine translocase deficiency, citrullinemia type I, hyperinsulinism-hyperammonemia syndrome, hyperornithinemia-hyperammonemia-homocitrullinuria syndrome, isovaleric aciduria, lysinuric protein intolerance, malonic aciduria, methylmalonic aciduria, methylmalonic aciduria due to cobalamin-related disorders, propionic acidemia, pyruvate carboxylase deficiency, and short chain acyl CoA dehydrogenase deficiency (SCAD deficiency). Many of these inborn errors of metabolism are associated with urea cycle disorders or impairment of amino acid metabolism. High levels of ammonia in the blood (hyperammonemia) lead to the activation of NMDA receptors in the brain. This results in the depletion of brain ATP, which in turn leads to the release of glutamate. Ammonia also leads to the impairment of mitochondrial function and calcium homeostasis, thereby decreasing ATP synthesis. Excess ammonia also increases the formation of nitric oxide (NO), which in turn reduces the activity of glutamine synthetase, and thereby decreases the elimination of ammonia in the brain (PMID: 12020609). As a neurotoxin, ammonia predominantly affects astrocytes. Disturbed mitochondrial function and oxidative stress, factors implicated in the induction of the mitochondrial permeability transition, appear to be involved in the mechanism of ammonia neurotoxicity. Ammonia can also affect the glutamatergic and GABAergic neuronal systems, the two prevailing neuronal systems of the cortical structures. All of these effects can lead to irreversible brain damage, coma, and/or death. Infants with urea cycle disorders and hyperammonemia initially exhibit vomiting and increasing lethargy. If untreated, seizures, hypotonia (poor muscle tone, floppiness), respiratory distress (respiratory alkalosis), and coma can occur. Adults with urea cycle disorders and hyperammonemia will exhibit episodes of disorientation, confusion, slurred speech, unusual and extreme combativeness or agitation, stroke-like symptoms, lethargy, and delirium. Ammonia also has toxic effects when an individual is exposed to ammonia solutions. Acute exposure to high levels of ammonia in air may be irritating to skin, eyes, throat, and lungs and cause coughing and burns. Lung damage and death may occur after exposure to very high concentrations of ammonia. Swallowing concentrated solutions of ammonia can cause burns in the mouth, throat, and stomach. Splashing ammonia into eyes can cause burns and even blindness.
7664-41-7
C00014
222
16134
AMMONIA
217
N
H3N
InChI=1S/H3N/h1H3
QGZKDVFQNNGYKY-UHFFFAOYSA-N
ammonia
17.0305
17.026549101
1
ammonia
0
1
FDB003908
Ammonia anhydrous;Ammonia inhalant;Ammonia solution strong [usan];Ammonia water;Ammoniak;Liquid ammonia;Am-fol;Ammonia;Ammonia (conc 20% or greater);Ammonia gas;Ammonia solution;Ammonia solution strong (nf);Ammonia water (jp15);Ammoniac [french];Ammoniaca [italian];Ammoniacum gummi;Ammoniak [german];Ammoniak kconzentrierter;Ammoniakgas;Ammonium ion;Amoniak [polish];Anhydrous ammonia;Aromatic ammonia vaporole;Azane;Nh(3);Nh3;Nitro-sil;Primaeres amin;Sekundaeres amin;Spirit of hartshorn;Tertiaeres amin;[nh3];Ammoniac;Amoniaco;R-717;Ammonia solution strong
PW_C000035
NH3
97
9
112
5
133
8
142
4
438
2
479
13
550
14
1468
54
2533
22
2572
3
5338
111
6016
147
7022
160
7177
205
11786
198
11848
277
11885
215
12708
291
12718
292
76966
225
77046
294
77329
133
77343
132
77469
333
77499
113
77539
334
77597
115
77985
347
77993
112
78072
329
79244
293
80650
135
80657
119
116203
109
119921
122
120049
408
120053
126
120136
407
120343
406
120363
412
120462
405
121046
124
121161
425
122119
382
122800
374
122805
443
122993
120
123010
446
123096
376
123610
118
123733
460
124671
399
125311
297
125427
482
125431
301
125502
481
125663
479
125708
478
126102
299
126274
484
126966
502
126970
207
127039
206
127158
501
127200
209
127600
388
127837
389
724
Cystathionine beta-synthase
P35520
Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury (By similarity).
HMDBP00779
CBS
21q22.3
BC011381
1
4.2.1.22
346
8
1829
2
511
Cystathionine gamma-lyase
P32929
Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function.
HMDBP00538
CTH
1p31.1
BC015807
1
4.4.1.1
338
8
1869
2
98631
7
83
Cystathionine beta-synthase
1
PW_P000083
97
724
4
46
1148
1
343
8
82
Cystathionine gamma-lyase
1
PW_P000082
96
511
4
45
1148
1
335
8
815
false
PW_R000815
Right
3303
590
1
Compound
false
3304
120
1
Compound
false
3305
1420
1
Compound
true
3306
67
1
Compound
false
356
83
4.2.1.22
816
false
PW_R000816
Right
3307
67
1
Compound
false
3308
1420
1
Compound
true
3309
448
1
Compound
false
3310
3
1
Compound
false
3311
35
1
Compound
true
363
82
4.4.1.1
1674
590
8
81
false
425
360
10
regular
200
190
1675
120
8
81
false
890
360
10
regular
200
190
1676
1420
8
49
false
845
810
10
regular
78
78
1677
67
8
81
false
655
935
10
regular
200
190
1678
1148
8
9
false
700
655
20
regular
100
35
1679
1420
8
49
false
850
1135
10
regular
78
78
1680
448
8
81
false
658
1535
10
regular
200
190
1681
3
8
81
false
448
1360
10
regular
200
190
1682
35
8
63
false
854
1366
10
regular
78
78
1683
1148
8
9
false
705
1247
19
regular
100
35
632
724
8
8
false
685
660
8
subunit
regular
140
85
633
511
8
8
false
685
1252
8
subunit
regular
140
85
585
83
36
8
625
632
253
1678
2409
Cofactor
586
82
36
8
626
633
254
1683
2415
Cofactor
2405
M625 455 C715 456 755 559 755 660
5
false
18
2406
M890 455 C813 458 756 558 755 660
5
false
18
2407
M845 849 C798 849 757 801 755 745
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
2408
M755 935 C755 905 755 775 755 745
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
2409
M250 250 L250 300 L300 250 z
10
true
18
2410
M755 1125 C755 1155 755 1222 755 1252
5
false
18
2411
M850 1174 C803 1177 752 1219 755 1252
5
false
18
2412
M758 1535 C758 1505 755 1367 755 1337
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
2413
M648 1455 C697 1455 756 1419 755 1337
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
2414
M854 1405 C810 1404 753 1402 755 1337
5
false
18
true
M 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345
false
2415
M250 250 L250 300 L300 250 z
10
true
18
7530
M525 360 C525 330 525 310 525 280
5
false
18
true
M 482.5 337.0096189432334 L 490 350 L 497.5 337.0096189432334
false
7531
M425 455 C395 455 385 455 355 455
5
false
18
true
M 427.0096189432334 406.5 L 440 399 L 427.0096189432334 391.5
false
7532
M990 360 C990 330 990 305 990 275
5
false
18
true
M 847.9903810567666 352.5 L 835 360 L 847.9903810567666 367.5
false
7533
M448 1455 C418 1455 378 1455 348 1455
5
false
18
true
M 295.9903810567666 1427.5 L 283 1435 L 295.9903810567666 1442.5
false
7534
M658 1630 C628 1630 563 1630 533 1630
5
false
18
true
M 445.9903810567666 1522.5 L 433 1530 L 445.9903810567666 1537.5
false
7535
M758 1725 C758 1755 758 1795 758 1825
5
false
18
true
M 600.5 1672.0096189432334 L 608 1685 L 615.5 1672.0096189432334
false
7536
M858 1630 C888 1630 923 1630 953 1630
5
false
18
true
M 755.0096189432334 1537.5 L 768 1530 L 755.0096189432334 1522.5
false
498
36
815
8
1839
1674
2405
Left
1840
1675
2406
Left
1841
1676
2407
Right
1842
1677
2408
Right
477
356
585
499
36
816
8
1843
1677
2410
Left
1844
1679
2411
Left
1845
1680
2412
Right
1846
1681
2413
Right
1847
1682
2414
Right
478
363
586
283
246
36
14
false
450
210
16
regular
265
1674
7530
Right
284
247
36
14
false
205
420
16
regular
266
1674
7531
Right
285
248
36
14
false
915
205
16
regular
267
1675
7532
Right
286
249
36
14
false
198
1420
16
regular
268
1681
7533
Left
287
250
36
14
false
383
1595
16
regular
269
1680
7534
Left
288
251
36
14
false
683
1825
16
regular
270
1680
7535
Left
289
252
36
14
false
953
1595
16
regular
271
1680
7536
Left
187146
210
634
1.3
1.3
0
3
14
327
267
479840
545
781
1.3
1.3
65
2
3
280
360
109
M125 225 C125 175 175 125 225 125 C482 125 817 125 1074 125 C1124 125 1174 175 1174 225 C1174 725 1174 1375 1174 1875 C1174 1925 1124 1975 1074 1975 C817 1975 482 1975 225 1975 C175 1975 125 1925 125 1875 C125 1375 125 725 125 225
1
true
6
1049.0
1850.0
888
235
Intracellular Space
620
265
20
1.3
1.3
200
15