2VBG
The complex structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis with 2R-1-hydroxyethyl-deazaThDP
Summary for 2VBG
| Entry DOI | 10.2210/pdb2vbg/pdb |
| Related | 2VBF |
| Descriptor | BRANCHED-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 Keywords | kdca, flavoprotein, thdp-dependent enzymes, thiamine pyrophosphate, lyase |
| Biological source | LACTOCOCCUS LACTIS |
| Total number of polymer chains | 2 |
| Total formula weight | 127796.43 |
| 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 citation | Berthold, 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: 18084069DOI: 10.1107/S0907444907050433 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
