2vjy | pdb_00002vjy
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
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Pages with broken file links
- 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
