2vk1
From Proteopedia
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===CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE PYRUVATE DECARBOXYLASE VARIANT D28A IN COMPLEX WITH ITS SUBSTRATE=== | ===CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE PYRUVATE DECARBOXYLASE VARIANT D28A IN COMPLEX WITH ITS SUBSTRATE=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[2vk1]] is a 4 chain structure of [[Pyruvate decarboxylase]] with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK1 OCA]. | |
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| + | ==See Also== | ||
| + | *[[Pyruvate decarboxylase|Pyruvate decarboxylase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019246454</ref><references group="xtra"/> |
[[Category: Pyruvate decarboxylase]] | [[Category: Pyruvate decarboxylase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: Weik, M.]] | [[Category: Weik, M.]] | ||
[[Category: Weiss, M S.]] | [[Category: Weiss, M S.]] | ||
| - | [[Category: Acetylation]] | ||
[[Category: Allosteric enzyme]] | [[Category: Allosteric enzyme]] | ||
[[Category: Asymmetric active site]] | [[Category: Asymmetric active site]] | ||
[[Category: Branched-chain amino acid catabolism]] | [[Category: Branched-chain amino acid catabolism]] | ||
| - | [[Category: Cytoplasm]] | ||
[[Category: Decarboxylase]] | [[Category: Decarboxylase]] | ||
[[Category: Dimer of dimer]] | [[Category: Dimer of dimer]] | ||
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[[Category: Tpp]] | [[Category: Tpp]] | ||
[[Category: Tryptophan catabolism]] | [[Category: Tryptophan catabolism]] | ||
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Revision as of 12:16, 26 July 2012
Contents |
CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE PYRUVATE DECARBOXYLASE VARIANT D28A IN COMPLEX WITH ITS SUBSTRATE
Template:ABSTRACT PUBMED 19246454
About this Structure
2vk1 is a 4 chain structure of Pyruvate decarboxylase with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
See Also
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
Categories: Pyruvate decarboxylase | Saccharomyces cerevisiae | Konig, S. | Kutter, S. | Weik, M. | Weiss, M S. | Allosteric enzyme | Asymmetric active site | Branched-chain amino acid catabolism | Decarboxylase | Dimer of dimer | Lyase | Magnesium | Metal-binding | Nucleus | Phenylalanine catabolism | Phosphorylation | Pyruvate | Substrate activation | Tdp | Thiamine diphosphate | Thiamine pyrophosphate | Tpp | Tryptophan catabolism
