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Literature summary for 3.7.1.14 extracted from

  • Li, J.J.; Li, C.; Blindauer, C.A.; Bugg, T.D.
    Evidence for a gem-diol reaction intermediate in bacterial C-C hydrolase enzymes BphD and MhpC from 13C NMR spectroscopy (2006), Biochemistry, 45, 12461-12469.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
H114A MhpC mutant is able to accept the 2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid, on a shorter time scale Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0238
-
2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid pH 8.0, 25°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid + H2O MhpC mutant is able to accept the 2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid, on a shorter time scale Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
MhpC
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.036
-
2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid pH 8.0, 25°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.51
-
2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid pH 8.0, 25°C Escherichia coli