2vjy
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
{{Seed}} | {{Seed}} | ||
- | [[Image:2vjy. | + | [[Image:2vjy.png|left|200px]] |
<!-- | <!-- | ||
Line 12: | Line 12: | ||
===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=== | ||
+ | |||
+ | <!-- | ||
+ | The line below this paragraph, {{ABSTRACT_PUBMED_19246454}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 19246454 is the PubMed ID number. | ||
+ | --> | ||
+ | {{ABSTRACT_PUBMED_19246454}} | ||
==About this Structure== | ==About this Structure== | ||
2VJY is a 4 chains structure of sequences 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]. | 2VJY is a 4 chains structure of sequences 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]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:19246454</ref><references group="xtra"/> | ||
[[Category: Kluyveromyces lactis]] | [[Category: Kluyveromyces lactis]] | ||
[[Category: Pyruvate decarboxylase]] | [[Category: Pyruvate decarboxylase]] | ||
Line 36: | Line 45: | ||
[[Category: Thiamine pyrophosphate]] | [[Category: Thiamine pyrophosphate]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 11 10:58:32 2009'' |
Revision as of 08:58, 11 March 2009
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
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