3phm
From Proteopedia
Contents |
REDUCED (CU+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM)
Template:ABSTRACT PUBMED 10504734
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
3phm is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
- Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM. Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase. Nat Struct Biol. 1999 Oct;6(10):976-83. PMID:10504734 doi:10.1038/13351
