3mlk: Difference between revisions
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{{STRUCTURE_3mlk| PDB=3mlk | SCENE= }} | {{STRUCTURE_3mlk| PDB=3mlk | SCENE= }} | ||
===Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite=== | ===Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite=== | ||
{{ABSTRACT_PUBMED_20958070}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/AMD_RAT 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. | |||
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:020958070</ref><references group="xtra"/><references/> | ||
[[Category: Peptidylglycine monooxygenase]] | [[Category: Peptidylglycine monooxygenase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: Eipper, B A.]] | [[Category: Eipper, B A.]] | ||
[[Category: Mains, R E.]] | [[Category: Mains, R E.]] | ||
[[Category: Ascorbate]] | |||
[[Category: Bioactive peptide activation]] | |||
[[Category: Monooxygenase]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 20:50, 17 April 2013
Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite
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
3mlk is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
- 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
