1mok

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[[Image:1mok.png|left|200px]]
 
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{{STRUCTURE_1mok| PDB=1mok | SCENE= }}
{{STRUCTURE_1mok| PDB=1mok | SCENE= }}
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===NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE===
===NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE===
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{{ABSTRACT_PUBMED_12390015}}
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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_12390015}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:012390015</ref><references group="xtra"/>
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<ref group="xtra">PMID:012390015</ref><references group="xtra"/><references/>
[[Category: Xanthobacter autotrophicus]]
[[Category: Xanthobacter autotrophicus]]
[[Category: Clark, D D.]]
[[Category: Clark, D D.]]

Revision as of 10:29, 16 April 2014

Template:STRUCTURE 1mok

Contents

NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE

Template:ABSTRACT PUBMED 12390015

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

1mok is a 4 chain structure with sequence from Xanthobacter autotrophicus. Full crystallographic information is available from OCA.

Reference

  • Nocek B, Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW. Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. Biochemistry. 2002 Oct 29;41(43):12907-13. PMID:12390015

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OCA

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