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3phm
From Proteopedia
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{{STRUCTURE_3phm| PDB=3phm | SCENE= }} | {{STRUCTURE_3phm| PDB=3phm | SCENE= }} | ||
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===REDUCED (CU+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM)=== | ===REDUCED (CU+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM)=== | ||
| + | {{ABSTRACT_PUBMED_10504734}} | ||
| - | + | ==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== | ||
| - | + | [[3phm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PHM OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:010504734</ref><references group="xtra"/><references/> |
[[Category: Peptidylglycine monooxygenase]] | [[Category: Peptidylglycine monooxygenase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: Ascorbate]] | [[Category: Ascorbate]] | ||
[[Category: Bioactive peptide activation]] | [[Category: Bioactive peptide activation]] | ||
| - | [[Category: Copper]] | ||
[[Category: Monooxygenase]] | [[Category: Monooxygenase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:19:18 2009'' | ||
Revision as of 08:07, 8 May 2013
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
