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2vjy
From Proteopedia
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[[Image:2vjy.png|left|200px]] | [[Image:2vjy.png|left|200px]] | ||
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{{STRUCTURE_2vjy| PDB=2vjy | SCENE= }} | {{STRUCTURE_2vjy| PDB=2vjy | SCENE= }} | ||
===PYRUVATE DECARBOXYLASE FROM KLUYVEROMYCES LACTIS IN COMPLEX WITH THE SUBSTRATE ANALOGUE METHYL ACETYLPHOSPHONATE=== | ===PYRUVATE DECARBOXYLASE FROM KLUYVEROMYCES LACTIS IN COMPLEX WITH THE SUBSTRATE ANALOGUE METHYL ACETYLPHOSPHONATE=== | ||
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{{ABSTRACT_PUBMED_19246454}} | {{ABSTRACT_PUBMED_19246454}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[2vjy]] is a 4 chain structure of [[Pyruvate decarboxylase]] with sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VJY 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: Kluyveromyces lactis]] | [[Category: Kluyveromyces lactis]] | ||
[[Category: Pyruvate decarboxylase]] | [[Category: Pyruvate decarboxylase]] | ||
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[[Category: Thiamine diphosphate]] | [[Category: Thiamine diphosphate]] | ||
[[Category: Thiamine pyrophosphate]] | [[Category: Thiamine pyrophosphate]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 6 09:24:26 2009'' | ||
Revision as of 06:26, 27 July 2012
Contents |
PYRUVATE DECARBOXYLASE FROM KLUYVEROMYCES LACTIS IN COMPLEX WITH THE SUBSTRATE ANALOGUE METHYL ACETYLPHOSPHONATE
Template:ABSTRACT PUBMED 19246454
About this Structure
2vjy is a 4 chain structure of Pyruvate decarboxylase with sequence from Kluyveromyces lactis. 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: 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
