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3mll
From Proteopedia
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{{STRUCTURE_3mll| PDB=3mll | SCENE= }} | {{STRUCTURE_3mll| PDB=3mll | SCENE= }} | ||
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===Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide=== | ===Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide=== | ||
| + | {{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 21:16, 17 April 2013
Contents |
Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide
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
3mll 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
