| EC |
1.2.1.59 |
| Accepted name: |
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) |
| Reaction: |
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H + H+ |
| Other name(s): |
triosephosphate dehydrogenase (NAD(P)); glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating) |
| Systematic name: |
D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating) |
| Comments: |
NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 39369-25-0 |
| References: |
| 1. |
Valverde, F., Losada, M. and Serrano, A. Cloning by functional complementation in E. coli of the gap2 gene of Synechocystis PCC 6803 supports an amphibolic role for cyanobacterial NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. In: P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, pp. 959–962. |
| 2. |
Valverde, F., Losada, M. and Serrano, A. 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. J. Bacteriol. 179 (1997) 4513–4522. [DOI] [PMID: 9226260] |
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| [EC 1.2.1.59 created 1999] |
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