Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

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.
    View publication on PubMed

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