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Literature summary for 1.2.1.107 extracted from

  • Veress, L.; Mullin, D.; Bovarsky, D.; Dimaunahan, C.; Byers, L.
    The role of His-176 in the chemical mechanism and thermal stability of glyceraldehyde-3-phosphate dehydrogenase (1996), FASEB J., 10, A1385.
No PubMed abstract available
Search for more literature for 1.2.1.107

Protein Variants

Protein Variants Comment Organism
H176N the mutant shows a Km value 5times smaller than for the wild type enzyme while the Km value for arsenate is about 5times larger. The mutant has a significantly reduced thermal stability at 65°C. The half-life for thermal denaturation for the mutant holoenzyme is increased nearly 100fold over the corresponding value for the apoenzyme Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + arsenate + NAD+ Geobacillus stearothermophilus
-
 1-arsono-3-phospho-D-glycerate + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + arsenate + NAD+
-
 Geobacillus stearothermophilus 1-arsono-3-phospho-D-glycerate + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
GPD
-
 Geobacillus stearothermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
100
-
 D-glyceraldehyde 3-phosphate mutant enzyme H176N, at pH 8.5 and 27°C Geobacillus stearothermophilus
100
-
 D-glyceraldehyde 3-phosphate wild type enzyme, at pH 8.5 and 27°C Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Geobacillus stearothermophilus