EC number:1.2.1.59
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.2 Acting on the aldehyde or oxo group of donors |
| 1.2.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.2.1.59 | ||
|---|---|---|---|
| Description: | Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating). | ||
| Alternative Name: |
Triosephosphate dehydrogenase (NAD(P)). Triosephosphate dehydrogenase (NAD(P)(+)). NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. | ||
| Prosite: | PDOC00069; | ||
| PDB: |
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| Cath: | 3.30.360.10; 3.40.50.720; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.2.1.59 |
| BRENDA Enzyme Link: | BRENDA 1.2.1.59 |
| KEGG Enzyme Link: | KEGG1.2.1.59 |
| BioCyc Enzyme Link: | BioCyc 1.2.1.59 |
| ExPASy Enzyme Link: | ExPASy1.2.1.59 |
| EC2PDB Enzyme Link: | EC2PDB 1.2.1.59 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.2.1.59 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.2.1.59 |
| IntEnz Enzyme Link: | IntEnz 1.2.1.59 |
| MEDLINE Enzyme Link: | MEDLINE 1.2.1.59 |
| RHEA:10300 | D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = 3-phospho-D-glyceroyl phosphate + H(+) + NADH |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[n+;H0:4]1:[cH;+0:5]:[cH;+0:6]:[cH;+0:7]:[c;H0;+0:8](-[*:9]):[cH;+0:10]:1.[*:11]=[CH;+0:12]-[*:13]>>[*:3]-[N;H0;+0:4]1-[CH;+0:5]=[CH;+0:6]-[CH2;+0:7]-[C;H0;+0:8](-[*:9])=[CH;+0:10]-1.[*:11]=[C;H0;+0:12](-[*:13])-[O;H0;+0:2]-[*:1] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803. | Valverde F, Losada M, Serrano A | 1997 Jul | 9226260 |
| Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. | Fillinger S, Boschi-Muller S, Azza S, Dervyn E, Branlant G, Aymerich S | 2000 May 12 | 10799476 |
| RHEA:10296 | D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = 3-phospho-D-glyceroyl phosphate + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[n+;H0:4]1:[cH;+0:5]:[cH;+0:6]:[cH;+0:7]:[c;H0;+0:8](-[*:9]):[cH;+0:10]:1.[*:11]=[CH;+0:12]-[*:13]>>[*:3]-[N;H0;+0:4]1-[CH;+0:5]=[CH;+0:6]-[CH2;+0:7]-[C;H0;+0:8](-[*:9])=[CH;+0:10]-1.[*:11]=[C;H0;+0:12](-[*:13])-[O;H0;+0:2]-[*:1] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803. | Valverde F, Losada M, Serrano A | 1997 Jul | 9226260 |
| Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. | Fillinger S, Boschi-Muller S, Azza S, Dervyn E, Branlant G, Aymerich S | 2000 May 12 | 10799476 |