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Literature summary for 1.2.1.9 extracted from

  • Marchal, S.; Branlant, G.
    Characterization of the amino acids involved in substrate specificity of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (2002), J. Biol. Chem., 277, 39235-39242.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
R124L turnover number is 21fold lower than turnover-number of wild-type enzym Streptococcus mutans
R301L turnover number is 1000fold lower than turnover-number of wild-type enzyme. Rate limiting step is acylation, compared to deacylation in wild-type enzyme Streptococcus mutans
R459I turnover number is 214fold lower than turnover-number of wild-type enzyme. Rate limiting step is acylation, compared to deacylation in wild-type enzyme Streptococcus mutans
Y170F turnover number is 1.7fold higher than turnover-number of wild-type enzyme Streptococcus mutans

Inhibitors

Inhibitors Comment Organism Structure
D-Glyceraldehyde-3-phosphate
-
Streptococcus mutans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.046
-
D-Glyceraldehyde-3-phosphate pH 8.5, 25┬░C, wild-type enzyme Streptococcus mutans
0.18
-
D-Glyceraldehyde-3-phosphate pH 8.5, 25┬░C, mutant enzyme Y170F Streptococcus mutans
9.2
-
D-Glyceraldehyde-3-phosphate pH 8.5, 25┬░C, mutant enzyme R459I Streptococcus mutans

Organism

Organism UniProt Comment Textmining
Streptococcus mutans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde-3-phosphate + NADP+ rate-limiting step in wild-type enzyme and in mutant enzymes R124L, and Y170F is deacylation. Rate limiting step in mutant enzymes R301L and R459I is acylation Streptococcus mutans D-3-phosphoglycerate + NADPH
-
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Synonyms

Synonyms Comment Organism
nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
Streptococcus mutans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.06
-
D-Glyceraldehyde-3-phosphate pH 8.5, 25┬░C, mutant enzyme R301L Streptococcus mutans
0.28
-
D-Glyceraldehyde-3-phosphate pH 8.5, 25┬░C, mutant enzyme R459I Streptococcus mutans
2.8
-
D-Glyceraldehyde-3-phosphate pH 8.5, 25┬░C, mutant enzyme R124L Streptococcus mutans
60
-
D-Glyceraldehyde-3-phosphate pH 8.5, 25┬░C, wild-type enzyme Streptococcus mutans
103
-
D-Glyceraldehyde-3-phosphate pH 8.5, 25┬░C, mutant enzyme Y170F Streptococcus mutans

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Streptococcus mutans

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.54
-
D-Glyceraldehyde-3-phosphate pH 8.4, 25┬░C, wild-type enzyme Streptococcus mutans
1.9
-
D-Glyceraldehyde-3-phosphate pH 8.4, 25┬░C, mutant enzyme R459I Streptococcus mutans