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Literature summary for 1.2.1.12 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
Search for more literature for 1.2.1.12

Protein Variants

Protein Variants Comment Organism
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
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
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Bacillus subtilis 3-phospho-D-glyceroyl phosphate + NADH
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+ glycolytic enzyme Bacillus subtilis 3-phospho-D-glyceroyl phosphate + NADH
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 Bacillus subtilis 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r
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]

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Bacillus subtilis
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