2vjy
From Proteopedia
PYRUVATE DECARBOXYLASE FROM KLUYVEROMYCES LACTIS IN COMPLEX WITH THE SUBSTRATE ANALOGUE METHYL ACETYLPHOSPHONATE
Template:ABSTRACT PUBMED 19246454
About this Structure
2VJY is a 4 chains structure of sequences from Kluyveromyces lactis. Full crystallographic information is available from OCA.
Reference
- Kutter S, Weiss MS, Wille G, Golbik R, Spinka M, Konig S. Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation. J Biol Chem. 2009 May 1;284(18):12136-44. Epub 2009 Feb 26. PMID:19246454 doi:10.1074/jbc.M806228200
Page seeded by OCA on Wed Mar 11 10:58:32 2009
Categories: Kluyveromyces lactis | Pyruvate decarboxylase | Konig, S. | Kutter, S. | Weiss, M S. | Wille, G. | Asymmetric active site | Decarboxylase | Dimer of dimer | Flavoprotein | Lyase | Magnesium | Map | Metal-binding | Methyl acetylphosphonate | Methylacetylphosphonate | Pyruvate | Substrate activation | Thiamine diphosphate | Thiamine pyrophosphate