3mlj | pdb_00003mlj

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Template:STRUCTURE 3mlj

Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)

Template:ABSTRACT PUBMED 20958070

Function

[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 Structure

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

Reference

  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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