Literature summary extracted from
Berthold, C.L.; Gocke, D.; Wood, M.D.; Leeper, F.J.; Pohl, M.; Schneider, G.
Structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction (2007), Acta Crystallogr. Sect. D, 63, 1217-1224.
Application
EC Number |
Application |
Comment |
Organism |
---|
4.1.1.72 |
synthesis |
the enzyme is able to catalyze carboligation reactions with an exceptionally broad substrate range, a feature that makes KdcA a potentially valuable biocatalyst for C-C bond formation, in particular for the enzymatic synthesis of diversely substituted 2-hydroxyketones with high enantioselectivity |
Lactococcus lactis |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.1.1.72 |
expressed in Escherichia coli strain BL21(DE3) |
Lactococcus lactis |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.1.1.72 |
hanging drop vapour diffusion method using 25-26% (v/v) PEG 200 in 0.1 M MES buffer pH 6.2 as a precipitant |
Lactococcus lactis |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
4.1.1.72 |
2-[(R)-1-hydroxyethyl]deaza thiamine diphosphate |
0.1 mM |
Lactococcus lactis |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
4.1.1.72 |
Mg2+ |
dependent |
Lactococcus lactis |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.1.72 |
Lactococcus lactis |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.1.1.72 |
Ni-NTA column chromatography |
Lactococcus lactis |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.1.1.72 |
3-methyl-2-oxobutanoic acid |
- |
Lactococcus lactis |
2-methylpropanal + CO2 |
- |
? |
|
4.1.1.72 |
additional information |
the enzyme is also able to catalyze carboligation reactions with an exceptionally broad substrate range, a feature that makes KdcA a potentially valuable biocatalyst for C-C bond formation, in particular for the enzymatic synthesis of diversely substituted 2-hydroxyketones with high enantioselectivity |
Lactococcus lactis |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.1.1.72 |
homodimer |
x-ray crystallography |
Lactococcus lactis |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.1.1.72 |
branched-chain keto acid decarboxylase |
- |
Lactococcus lactis |
4.1.1.72 |
KdcA |
- |
Lactococcus lactis |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.1.1.72 |
thiamine diphosphate |
dependent |
Lactococcus lactis |
|