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Literature summary for 1.2.1.72 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

Protein Variants Comment Organism
C149A no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity Escherichia coli
C149G no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity Escherichia coli
C149V no significant phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity Escherichia coli
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
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
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
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
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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
recombinant
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
14.7
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
additional information the enzyme also shows low phosphorylating glyceraldehyde-3-phosphate dehydrogenase activity Escherichia coli ?
-
?

Subunits

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

Synonyms

Synonyms Comment Organism
GapB-encoded protein
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.21
-
NAD+ 25°C, mutant enzyme H176N Escherichia coli
0.21
-
D-erythrose 4-phosphate 25°C, mutant enzyme H176N Escherichia coli
0.6
-
NAD+ 25°C, mutant enzyme C311Y Escherichia coli
0.6
-
D-erythrose 4-phosphate 25°C, mutant enzyme C311Y Escherichia coli
3.5
-
NAD+ 25°C, mutant enzyme C311A Escherichia coli
3.5
-
D-erythrose 4-phosphate 25°C, mutant enzyme C311A Escherichia coli
4
-
NAD+ 25°C, mutant enzyme M179T Escherichia coli
4
-
D-erythrose 4-phosphate 25°C, mutant enzyme M179T Escherichia coli
7.4
-
NAD+ 25°C, mutant enzyme E32D Escherichia coli
7.4
-
D-erythrose 4-phosphate 25°C, mutant enzyme E32D Escherichia coli
20
-
NAD+ 25°C, wild-type enzyme Escherichia coli
20
-
D-erythrose 4-phosphate 25°C, wild-type enzyme Escherichia coli