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2VBG

The complex structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis with 2R-1-hydroxyethyl-deazaThDP

Summary for 2VBG
Entry DOI10.2210/pdb2vbg/pdb
Related2VBF
DescriptorBRANCHED-CHAIN ALPHA-KETOACID DECARBOXYLASE, MAGNESIUM ION, 2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-[(1R)-1-HYDROXYETHYL]-3-METHYL-2-THIENYL}ETHYL TRIHYDROGEN DIPHOSPHATE, ... (4 entities in total)
Functional Keywordskdca, flavoprotein, thdp-dependent enzymes, thiamine pyrophosphate, lyase
Biological sourceLACTOCOCCUS LACTIS
Total number of polymer chains2
Total formula weight127796.43
Authors
Berthold, C.L.,Gocke, D.,Wood, M.D.,Leeper, F.,Pohl, M.,Schneider, G. (deposition date: 2007-09-12, release date: 2007-11-27, Last modification date: 2023-12-13)
Primary citationBerthold, C.L.,Gocke, D.,Wood, M.D.,Leeper, F.,Pohl, M.,Schneider, G.
Crystal Structure of the Branched-Chain Keto Acid Decarboxylase (Kdca) from Lactococcus Lactis Provides Insights Into the Structural Basis for the Chemo- and Enantioselective Carboligation Reaction
Acta Crystallogr.,Sect.D, 63:1217-, 2007
Cited by
PubMed Abstract: The thiamin diphosphate (ThDP) dependent branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis catalyzes the decarboxylation of 3-methyl-2-oxobutanoic acid to 3-methylpropanal (isobutyraldehyde) and CO2. 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. The crystal structures of recombinant holo-KdcA and of a complex with an inhibitory ThDP analogue mimicking a reaction intermediate have been determined to resolutions of 1.6 and 1.8 A, respectively. KdcA shows the fold and cofactor-protein interactions typical of thiamin-dependent enzymes. In contrast to the tetrameric assembly displayed by most other ThDP-dependent decarboxylases of known structure, KdcA is a homodimer. The crystal structures provide insights into the structural basis of substrate selectivity and stereoselectivity of the enzyme and thus are suitable as a framework for the redesign of the substrate profile in carboligation reactions.
PubMed: 18084069
DOI: 10.1107/S0907444907050433
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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