2vk1 | pdb_00002vk1
From Proteopedia
CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE PYRUVATE DECARBOXYLASE VARIANT D28A IN COMPLEX WITH ITS SUBSTRATE
About this Structure
2VK1 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 10:55:34 2009
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Pages with broken file links
- 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
