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Literature summary extracted from

  • Zhao, G.; Pease, A.J.; Bharani, N.; 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 (1995), J. Bacteriol., 177, 2804-2812.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.1.72 additional information the enzyme requires the presence of a reducing agent, such as DTT or 2-mercaptoethanol, to maintain activity Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.72
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.72 0.074
-
NAD+
-
Escherichia coli
1.2.1.72 0.96
-
D-erythrose 4-phosphate
-
Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.72 37200
-
4 * 37200, SDS-PAGE Escherichia coli
1.2.1.72 132000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.72 D-erythrose 4-phosphate + NAD+ Escherichia coli the enzyme possible plays a role in the de novo biosynthesis of pyridoxal 5'-phosphate 4-phosphoerythronate + NADH
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.72 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.72
-
Escherichia coli

Storage Stability

EC Number Storage Stability Organism
1.2.1.72 4°C, stable for weeks with negligible loss of activity Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?

Subunits

EC Number Subunits Comment Organism
1.2.1.72 tetramer 4 * 37200, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.2.1.72 E4PDH
-
Escherichia coli
1.2.1.72 epd
-
Escherichia coli
1.2.1.72 gap2 renamed as epd Escherichia coli
1.2.1.72 GapB renamed as epd Escherichia coli
1.2.1.72 gapB-encoded dehydrogenase renamed as epd Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.72 50
-
at pH 8.6 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.1.72 50
-
stable below Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.72 169
-
NAD+
-
Escherichia coli
1.2.1.72 200
-
D-erythrose 4-phosphate
-
Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.72 7 10 the pH profile rises steeply between pH 7 and 9 and then drops slightly at pH 10 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.72 3-acetylpyridine adenine dinucleotide less efficient than NAD+ Escherichia coli
1.2.1.72 NAD+
-
Escherichia coli