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Literature summary extracted from

  • Boschi-Muller, S.; Azza, S.; Pollastro, D.; Corbier, C.; Branlant, G.
    Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase (1997), J. Biol. Chem., 272, 15106-15112.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.72 C149A no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity Escherichia coli
1.2.1.72 C149G no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity Escherichia coli
1.2.1.72 C149V no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity Escherichia coli
1.2.1.72 C311A mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 5.7fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+ Escherichia coli
1.2.1.72 C311Y mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 33.3fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+ Escherichia coli
1.2.1.72 E32D mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 2.7fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+ Escherichia coli
1.2.1.72 H176N turnover number of phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity is decreased by the factor 40. 95.2fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+ Escherichia coli
1.2.1.72 M179T mutation does not drastically change the phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity. 5fold decrease in turnover number for the activity with D-erythrose 4-phosphate and NAD+ Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.72 0.24
-
D-erythrose 4-phosphate 25°C, mutant enzyme H176N Escherichia coli
1.2.1.72 0.5
-
NAD+ 25°C, mutant enzyme H176N Escherichia coli
1.2.1.72 0.51
-
D-erythrose 4-phosphate 25°C, wild-type enzyme Escherichia coli
1.2.1.72 0.7
-
D-erythrose 4-phosphate 25°C, mutant enzyme C311Y Escherichia coli
1.2.1.72 0.7
-
D-erythrose 4-phosphate 25°C, mutant enzyme M179T Escherichia coli
1.2.1.72 0.8
-
NAD+ 25°C, wild-type enzyme Escherichia coli
1.2.1.72 0.8
-
D-erythrose 4-phosphate 25°C, mutant enzyme C311A Escherichia coli
1.2.1.72 1.9
-
D-erythrose 4-phosphate 25°C, mutant enzyme E32D Escherichia coli
1.2.1.72 2.3
-
NAD+ 25°C, mutant enzyme E32D Escherichia coli
1.2.1.72 3.5
-
NAD+ 25°C, mutant enzyme M179T Escherichia coli
1.2.1.72 4
-
NAD+ 25°C, mutant enzyme C311A Escherichia coli
1.2.1.72 5
-
NAD+ 25°C, mutant enzyme C311Y Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.72 37170
-
x * 37170, mass spectrometry Escherichia coli

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.72 recombinant Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.72 14.7
-
-
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 + 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 additional information the enzyme also shows low phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity Escherichia coli ?
-
?

Subunits

EC Number Subunits Comment Organism
1.2.1.72 ? x * 37170, mass spectrometry Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.2.1.72 GapB-encoded protein
-
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 0.21
-
NAD+ 25°C, mutant enzyme H176N Escherichia coli
1.2.1.72 0.21
-
D-erythrose 4-phosphate 25°C, mutant enzyme H176N Escherichia coli
1.2.1.72 0.6
-
NAD+ 25°C, mutant enzyme C311Y Escherichia coli
1.2.1.72 0.6
-
D-erythrose 4-phosphate 25°C, mutant enzyme C311Y Escherichia coli
1.2.1.72 3.5
-
NAD+ 25°C, mutant enzyme C311A Escherichia coli
1.2.1.72 3.5
-
D-erythrose 4-phosphate 25°C, mutant enzyme C311A Escherichia coli
1.2.1.72 4
-
NAD+ 25°C, mutant enzyme M179T Escherichia coli
1.2.1.72 4
-
D-erythrose 4-phosphate 25°C, mutant enzyme M179T Escherichia coli
1.2.1.72 7.4
-
NAD+ 25°C, mutant enzyme E32D Escherichia coli
1.2.1.72 7.4
-
D-erythrose 4-phosphate 25°C, mutant enzyme E32D Escherichia coli
1.2.1.72 20
-
NAD+ 25°C, wild-type enzyme Escherichia coli
1.2.1.72 20
-
D-erythrose 4-phosphate 25°C, wild-type enzyme Escherichia coli