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Structure paper

TitleAllosteric Activation of Pyruvate Decarboxylases. A Never-Ending Story.
Journal, issue, pagesJ. Mol. Catal. , B Enzym., Vol. 61, Page 100-, Year 2014
Publish dateDec 17, 2007 (structure data deposition date)
AuthorsKonig, S. / Spinka, M. / Kutter, S.
External linksJ. Mol. Catal. , B Enzym. / Search PubMed
MethodsX-ray diffraction
Resolution1.6 - 1.95 Å
Structure data

PDB-2vk4:
Crystal structure of pyruvate decarboxylase from Kluyveromyces lactis
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-2w93:
Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with the surrogate pyruvamide
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-TPP:
THIAMINE DIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PY0:
(1S,2S)-1-amino-1,2-dihydroxypropan-1-olate

Source
  • kluyveromyces lactis (yeast)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsLYASE / METAL-BINDING / DECARBOXYLASE / DIMER OF DIMERS / SUBSTRATE ACTIVATION / THIAMINE DIPHOSPHATE / TDP / TPP / MAGNESIUM / FLAVOPROTEIN / THIAMINE PYROPHOSPHATE / ASYMMETRIC ACTIVE SITES / SUBSTRATE REGULATION / NUCLEUS / CYTOPLASM / ACETYLATION / PHOSPHOPROTEIN / ALLOSTERIC ENZYME / PHENYLALANINE CATABOLISM / TRYPTOPHAN CATABOLISM / PYRUVATE DECARBOXYLASE / BRANCHED-CHAIN AMINO ACID CATABOLISM / THIOHEMIKETAL

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