Pyruvate decarboxylase from Kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate

methoxy-[(1~{R})-1-oxidanylethyl]phosphinic acid

Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation.

VAL C 324 HAS WRONG CHIRALITY AT ATOM CA

20MM CITRATE, 10% PEG2000, 10% PEG6000, 5MM TDP, 5MM MAGNESIUM SULFATE, 1MM DTT, 40MM METHYL ACETYLPHOSPHONATE, PH 6.1, 0.95MG KLPDC/ML, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 281K

CRYSTAL STRUCTURE OF PYRUVATE DECARBOXYLASE FROM KLUYVEROMYCES LACTIS

CRYSTAL STRUCTURE OF PYRUVATE DECARBOXYLASE FROMKLUYVEROMYCES LACTIS

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

METAL-BINDING, DECARBOXYLASE, DIMER OF DIMERS, METHYLACETYLPHOSPHONATE, METHYL ACETYLPHOSPHONATE, SUBSTRATE ACTIVATION, THIAMINE DIPHOSPHATE, THIAMINE PYROPHOSPHATE, ASYMMETRIC ACTIVE SITES, MAP, LYASE, PYRUVATE, MAGNESIUM, FLAVOPROTEIN