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2vk8
From Proteopedia
CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE PYRUVATE DECARBOXYLASE VARIANT E477Q IN COMPLEX WITH ITS SUBSTRATE
Template:ABSTRACT PUBMED 19246454
About this Structure
2VK8 is a 4 chains structure of sequences from Saccharomyces cerevisiae. 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 11:01:13 2009
Categories: Pyruvate decarboxylase | Saccharomyces cerevisiae | Konig, S. | Kutter, S. | Weik, M. | Weiss, M S. | Acetylation | Allosteric enzyme | Asymmetric active site | Branched-chain amino acid catabolism | Cytoplasm | Decarboxylase | Dimer of dimer | Lyase | Magnesium | Metal-binding | Nucleus | Phenylalanine catabolism | Phosphorylation | Pyruvate | Substrate activation | Tdp | Thiamine diphosphate | Thiamine pyrophosphate | Tpp | Tryptophan catabolism
