3q6j

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[[Image:3q6j.jpg|left|200px]]
 
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{{STRUCTURE_3q6j| PDB=3q6j | SCENE= }}
{{STRUCTURE_3q6j| PDB=3q6j | SCENE= }}
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===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===
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{{ABSTRACT_PUBMED_21192936}}
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==Function==
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[[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.
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{{ABSTRACT_PUBMED_21192936}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:21192936</ref><references group="xtra"/>
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<ref group="xtra">PMID:021192936</ref><references group="xtra"/><references/>
[[Category: Xanthobacter autotrophicus]]
[[Category: Xanthobacter autotrophicus]]
[[Category: Ensign, S A.]]
[[Category: Ensign, S A.]]
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[[Category: Pandey, A S.]]
[[Category: Pandey, A S.]]
[[Category: Peters, J W.]]
[[Category: Peters, J W.]]
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[[Category: Carbon dioxide]]
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[[Category: Carboxylase]]
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[[Category: Coenzyme m]]
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[[Category: Disulfide]]
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[[Category: Fad]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]

Revision as of 08:19, 8 May 2013

Template:STRUCTURE 3q6j

Contents

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

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OCA

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