3q6j: Difference between revisions
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{{STRUCTURE_3q6j| PDB=3q6j | SCENE= }} | {{STRUCTURE_3q6j| PDB=3q6j | SCENE= }} | ||
===Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M Oxidoreductase/Carboxylase=== | ===Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M Oxidoreductase/Carboxylase=== | ||
{{ABSTRACT_PUBMED_21192936}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/XECC_XANP2 XECC_XANP2]] Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M. | |||
==About this Structure== | ==About this Structure== | ||
| Line 22: | Line 10: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:021192936</ref><references group="xtra"/><references/> | ||
[[Category: Xanthobacter autotrophicus]] | [[Category: Xanthobacter autotrophicus]] | ||
[[Category: Ensign, S A.]] | [[Category: Ensign, S A.]] | ||
| Line 28: | Line 16: | ||
[[Category: Pandey, A S.]] | [[Category: Pandey, A S.]] | ||
[[Category: Peters, J W.]] | [[Category: Peters, J W.]] | ||
[[Category: Carbon dioxide]] | |||
[[Category: Carboxylase]] | |||
[[Category: Coenzyme m]] | |||
[[Category: Disulfide]] | |||
[[Category: Fad]] | |||
[[Category: Nadp]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 08:19, 8 May 2013
Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M Oxidoreductase/Carboxylase
Template:ABSTRACT PUBMED 21192936
Function
[XECC_XANP2] Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M.
About this Structure
3q6j is a 2 chain structure with sequence from Xanthobacter autotrophicus. Full crystallographic information is available from OCA.
Reference
- Pandey AS, Mulder DW, Ensign SA, Peters JW. Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase. FEBS Lett. 2011 Feb 4;585(3):459-64. Epub 2010 Dec 27. PMID:21192936 doi:10.1016/j.febslet.2010.12.035