2c3d
From Proteopedia
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Revision as of 14:51, 30 October 2007
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2.15 ANGSTROM CRYSTAL STRUCTURE OF 2-KETOPROPYL COENZYME M OXIDOREDUCTASE CARBOXYLASE WITH A COENZYME M DISULFIDE BOUND AT THE ACTIVE SITE
Overview
The structure of the mixed, enzyme-cofactor disulfide intermediate of, ketopropyl-coenzyme M oxidoreductase/carboxylase has been determined by, X-ray diffraction methods. Ketopropyl-coenzyme M, oxidoreductase/carboxylase belongs to a family of pyridine, nucleotide-containing flavin-dependent disulfide oxidoreductases, which, couple the transfer of hydride derived from the NADPH to the reduction of, protein cysteine disulfide. Ketopropyl-coenzyme M, oxidoreductase/carboxylase, a unique member of this enzyme class, catalyzes thioether bond cleavage of the substrate, 2-ketopropyl-coenzyme, M, and carboxylation of what is thought to be an enzyme-stabilized, enolacetone intermediate. The mixed disulfide of 2-ketopropyl-coenzyme M, oxidoreductase/carboxylase was captured through crystallization ... [(full description)]
About this Structure
2C3D is a [Single protein] structure of sequence from [Xanthobacter autotrophicus] with FAD and COM as [ligands]. Active as [2-oxopropyl-CoM reductase (carboxylating)], with EC number [1.8.1.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase., Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW, Biochemistry. 2006 Jan 10;45(1):113-20. PMID:16388586
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