Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fillinger, S.; Boschi-Muller, S.; Azza, S.; Dervyn, E.; Branlant, G.; Aymerich, S.
    Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (2000), J. Biol. Chem., 275, 14031-14037.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.12 D32A activity of mutant enzyme D32A with NAD+ is equal to that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 3% of the activity with NAD+ Bacillus subtilis
1.2.1.12 D32A/L187N wild-type enzyme has no activity with NADP+, the mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+ Bacillus subtilis
1.2.1.12 L187N activity of mutant L187N with NAD+ is higher than that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 7% of the activity with NAD+ Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.12 0.1
-
 NAD+ wild-type enzyme Bacillus subtilis
1.2.1.12 0.5
-
 NAD+ mutant enzyme D32A Bacillus subtilis
1.2.1.12 0.75
-
 NAD+ mutant enzyme D32A/L187N Bacillus subtilis
1.2.1.12 1
-
 NAD+ mutant enzyme L187N Bacillus subtilis
1.2.1.12 1.7
-
 NADP+ mutant enzyme D32A/L187N Bacillus subtilis
1.2.1.12 7.1
-
 NADP+ mutant enzyme D32A and L187N Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Bacillus subtilis glycolytic enzyme 3-phospho-D-glyceroyl phosphate + NADH
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.12 Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Bacillus subtilis 3-phospho-D-glyceroyl phosphate + NADH
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ glycolytic enzyme Bacillus subtilis 3-phospho-D-glyceroyl phosphate + NADH
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 Bacillus subtilis 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r
1.2.1.12 additional information wild-type enzyme has no activity with NADP+, the mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+ Bacillus subtilis ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.12 2
-
 NADP+ mutant enzyme D32A Bacillus subtilis
1.2.1.12 2.5
-
 NAD+ mutant enzyme D32A/L187N Bacillus subtilis
1.2.1.12 8
-
 NADP+ mutant enzyme L187N Bacillus subtilis
1.2.1.12 17.7
-
 NADP+ mutant enzyme D32A/L187N Bacillus subtilis
1.2.1.12 70
-
 NAD+ wild-type enzyme and mutant enzyme L187N Bacillus subtilis
1.2.1.12 112
-
 NAD+ mutant enzyme L187N Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.12 NAD+
-
 Bacillus subtilis
1.2.1.12 NADP+ wild-type enzyme has no activity with NADP+. The mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+. Activity of mutant enzyme D32A with NAD+ is equal to that of the wild-type enzyme. Activity of mutant L187N with NAD+ is higher than that of the wild-type enzyme. Mutant enzymes D32A and L187N also show activity with NADP+, 3-7% of the activity with NAD+ Bacillus subtilis