EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.2.1.72 | D-erythrose 4-phosphate + 3-acetylpyridine adenine dinucleotide |
- |
Escherichia coli |
4-phosphoerythronate + ? |
- |
? |
1.2.1.72 | D-erythrose 4-phosphate + NAD+ |
- |
Escherichia coli |
4-phosphoerythronate + NADH |
- |
? |
1.2.1.72 | D-erythrose 4-phosphate + NAD+ |
the enzyme possible plays a role in the de novo biosynthesis of pyridoxal 5'-phosphate |
Escherichia coli |
4-phosphoerythronate + NADH |
- |
? |
1.2.1.72 | D-erythrose 4-phosphate + NAD+ |
the chemical mechanism of erythrose 4-phosphate oxidation by gap-encoded protein proceeds through a two-step mechanism involving covalent intermediates with Cys149, with rates associated to the acylation and deacylation process of 280 per s and 20 per s, respectively. No isotopic solvent effect is observed, suggesting that the rate-limiting step is not hydrolysis |
Escherichia coli |
4-phosphoerythronate + NADH |
- |
? |
1.2.1.72 | D-erythrose 4-phosphate + NAD+ |
production of E4P can be coupled to the NADH generating E4PD activity which enables measurement of the transketolase reaction involving F6P as donor substrate |
Escherichia coli |
4-phosphoerythronate + NADH |
- |
? |
1.2.1.72 | D-ribose 5-phosphate + NAD+ |
D-Ribose 5-phosphate can be used as ketol acceptor substrate in the reaction although D-ribose 5-phosphate is also a substrate for the coupling enzyme |
Escherichia coli |
? + NADH |
- |
? |
1.2.1.72 | more |
enzyme is involved in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12 |
Escherichia coli |
? |
- |
? |
1.2.1.72 | more |
epd expression is very low in Escherichia coli. In presence of glucose, the 3 epd, pgk and fba ORFs are efficiently cotranscribed from promoter epd P0. Translational limitation of the epd expression in Escherichia coli |
Escherichia coli |
? |
- |
? |
1.2.1.72 | more |
expression of epd in Vibrio cholera is not regulated by iron, nor is it required for virulence in an infant model |
Vibrio cholerae serotype O1 |
? |
- |
? |
1.2.1.72 | more |
gapB is dispensable for glycolysis and pyridoxal biosynthesis pathway |
Escherichia coli |
? |
- |
? |