| EC |
1.2.1.72 |
| Accepted name: |
erythrose-4-phosphate dehydrogenase |
| Reaction: |
D-erythrose 4-phosphate + NAD+ + H2O = 4-phosphoerythronate + NADH + 2 H+ |
|
For diagram of pyridoxal biosynthesis, click here |
| Other name(s): |
erythrose 4-phosphate dehydrogenase; E4PDH; GapB; Epd dehydrogenase; E4P dehydrogenase |
| Systematic name: |
D-erythrose 4-phosphate:NAD+ oxidoreductase |
| Comments: |
This enzyme was originally thought to be a glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), but this has since been disproved, as glyceraldehyde 3-phosphate is not a substrate [1,2]. Forms part of the pyridoxal-5′-phosphate cofactor biosynthesis pathway in Escherichia coli, along with EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5′-phosphate synthase) and EC 1.4.3.5 (pyridoxamine-phosphate oxidase). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 131554-04-6 |
| References: |
| 1. |
Zhao, G., Pease, A.J., Bharani, N. and Winkler, M.E. Biochemical characterization of gapB-encoded erythrose 4-phosphate
dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal
5′-phosphate biosynthesis. J. Bacteriol. 177 (1995) 2804–2812. [DOI] [PMID: 7751290] |
| 2. |
Boschi-Muller, S., Azza, S., Pollastro, D., Corbier, C. and Branlant, G. Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate
dehydrogenase of Escherichia coli and phosphorylating
glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 272 (1997) 15106–15112. [DOI] [PMID: 9182530] |
| 3. |
Yang, Y., Zhao, G., Man, T.K. and Winkler, M.E. Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5′-phosphate coenzyme biosynthesis in Escherichia coli K-12. J. Bacteriol. 180 (1998) 4294–4299. [PMID: 9696782] |
|
| [EC 1.2.1.72 created 2006] |
| |
|
| |
|
Printable version