EC 1 - Oxidoreductases
EC 1.2 - Acting on the aldehyde or oxo group of donors
EC 1.2.1 - With NAD+ or NADP+ as acceptor
EC 1.2.1.72 - Erythrose-4-phosphate dehydrogenase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.2.1.72
Names
Accepted name:
erythrose-4-phosphate dehydrogenase
Other
names:
erythrose 4-phosphate dehydrogenase
E4PDH
GapB
Epd dehydrogenase
E4P dehydrogenase
E4PDH
GapB
Epd dehydrogenase
E4P dehydrogenase
Systematic name:
D-erythrose 4-phosphate:NAD+ oxidoreductase
Reaction
- D-erythrose 4-phosphate + NAD+ + H2O = 4-phosphoerythronate + NADH + 2 H+
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 coenzyme 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
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Protein domains and families:
PROSITE:PDOC00069
Gene Ontology:
GO:0048001
References
-
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 : 2804-2812 (1995). [PMID: 7751290]
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Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase.J. Biol. Chem. 272 : 15106-15112 (1997). [PMID: 9182530]
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Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12.J. Bacteriol. 180 : 4294-4299 (1998). [PMID: 9696782]
[EC 1.2.1.72 created 2006]