1cpo
From Proteopedia
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Revision as of 12:54, 30 October 2007
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CHLOROPEROXIDASE
Overview
BACKGROUND: Chloroperoxidase (CPO) is a versatile heme-containing enzyme, that exhibits peroxidase, catalase and cytochrome P450-like activities in, addition to catalyzing halogenation reactions. The structure determination, of CPO was undertaken to help elucidate those structural features that, enable the enzyme to exhibit these multiple activities. RESULTS: Despite, functional similarities with other heme enzymes, CPO folds into a novel, tertiary structure dominated by eight helical segments. The catalytic, base, required to cleave the peroxide O-O bond, is glutamic acid rather, than histidine as in other peroxidases. CPO contains a hydrophobic patch, above the heme that could be the binding site for substrates that undergo, P450-like reactions. The crystal structure also shows ... [(full description)]
About this Structure
1CPO is a [Single protein] structure of sequence from [Leptoxyphium fumago] with NAG, MAN, XYS, MN and HEM as [ligands]. Active as [Chloride peroxidase], with EC number [1.11.1.10]. Structure known Active Sites: HE1, HEM, MN, NG1, NG2, NG3, OG1, OG2, OG3, OG4, OG5, OG6, OG7, OG8, OG9, OGA and OGB. Full crystallographic information is available from [OCA].
Reference
The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid., Sundaramoorthy M, Terner J, Poulos TL, Structure. 1995 Dec 15;3(12):1367-77. PMID:8747463
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