3mif

Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)

Template:ABSTRACT PUBMED 20958070

FunctionFunction

[AMD_RAT] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.

About this StructureAbout this Structure

3mif is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Chufan EE, Prigge ST, Siebert X, Eipper BA, Mains RE, Amzel LM. Differential reactivity between two copper sites in peptidylglycine alpha-hydroxylating monooxygenase. J Am Chem Soc. 2010 Nov 10;132(44):15565-72. PMID:20958070 doi:10.1021/ja103117r

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OCA

[1] Chufan EE, Prigge ST, Siebert X, Eipper BA, Mains RE, Amzel LM. Differential reactivity between two copper sites in peptidylglycine alpha-hydroxylating monooxygenase. J Am Chem Soc. 2010 Nov 10;132(44):15565-72. PMID:20958070 doi:10.1021/ja103117r

[xtra 1]