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Literature summary extracted from

  • Yep, A.; Kenyon, G.L.; McLeish, M.J.
    Determinants of substrate specificity in KdcA, a thiamin diphosphate-dependent decarboxylase (2006), Bioorg. Chem., 34, 325-336.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.1 expression of enzyme mutants in Escherichia coli strain BL21(DE3) Lactococcus lactis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.1 F381W site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing high kcat and activity with pyruvate compared to the wild-type enzyme Lactococcus lactis
4.1.1.1 M538W site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing higher kcat and activity with pyruvate compared to the wild-type enzyme Lactococcus lactis
4.1.1.1 S286Y site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing high kcat and activity with pyruvate compared to the wild-type enzyme Lactococcus lactis
4.1.1.1 V461I site-directed mutagenesis, mutation of KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, alters the substrate specificity to a pyruvate decarboxylase showing higher kcat and activity with pyruvate compared to the wild-type enzyme Lactococcus lactis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.1 additional information
-
 additional information kinetics analysis of the wild-type enzyme with beta-hydroxypyruvate as substrate in the decarboxylation reaction Lactococcus lactis
4.1.1.1 18
-
 Pyruvic acid pH 6.0, 30°C, recombinant mutant V461I Lactococcus lactis
4.1.1.1 22
-
 Pyruvic acid pH 6.0, 30°C, recombinant mutant M538W Lactococcus lactis
4.1.1.1 34
-
 Pyruvic acid pH 6.0, 30°C, recombinant mutant S286Y Lactococcus lactis
4.1.1.1 65
-
 Pyruvic acid pH 6.0, 30°C, recombinant mutant F381W Lactococcus lactis

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.1 Lactococcus lactis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.1 recombinant enzyme mutants from Escherichia coli strain BL21(DE3) Lactococcus lactis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.1 2-oxohexanoic acid the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview Lactococcus lactis pentanal + CO2
-
 ?
4.1.1.1 2-oxopentanoic acid the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview Lactococcus lactis butanal + CO2
-
 ?
4.1.1.1 additional information substrate specificity of the engineered KdcA mutant enzymes with branched and unbranched 2-oxo acid substrates, overview Lactococcus lactis ?
-
 ?
4.1.1.1 pyruvic acid the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview Lactococcus lactis acetaldehyde + CO2
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.1 30
-
 assay at Lactococcus lactis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.1 2.3
-
 Pyruvic acid pH 6.0, 30C, recombinant mutant V461I Lactococcus lactis
4.1.1.1 2.5
-
 Pyruvic acid pH 6.0, 30C, recombinant mutant M538W Lactococcus lactis
4.1.1.1 17
-
 Pyruvic acid pH 6.0, 30C, recombinant mutant S286Y Lactococcus lactis
4.1.1.1 26
-
 Pyruvic acid pH 6.0, 30C, recombinant mutant F381W Lactococcus lactis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.1 6
-
-
 Lactococcus lactis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.1 thiamine diphosphate dependent on Lactococcus lactis