EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.1 | expression of enzyme mutants in Escherichia coli strain BL21(DE3) | Lactococcus lactis |
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 |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.1 | Lactococcus lactis | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.1 | recombinant enzyme mutants from Escherichia coli strain BL21(DE3) | Lactococcus lactis |
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 | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.1 | 30 | - |
assay at | Lactococcus lactis |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.1 | 6 | - |
- |
Lactococcus lactis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.1 | thiamine diphosphate | dependent on | Lactococcus lactis |