3mie

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[[Image:3mie.jpg|left|200px]]
 
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{{STRUCTURE_3mie| PDB=3mie | SCENE= }}
{{STRUCTURE_3mie| PDB=3mie | SCENE= }}
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===Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide obtained by soaking (50mM NaN3)===
===Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide obtained by soaking (50mM NaN3)===
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{{ABSTRACT_PUBMED_20958070}}
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==Function==
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[[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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{{ABSTRACT_PUBMED_20958070}}
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==About this Structure==
==About this Structure==
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3MIE 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=3MIE OCA].
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[[3mie]] 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=3MIE OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:20958070</ref><references group="xtra"/>
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<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: Monooxygenase]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 24 14:15:07 2010''
 

Revision as of 20:54, 17 April 2013

Template:STRUCTURE 3mie

Contents

Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide obtained by soaking (50mM NaN3)

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

3mie 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

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OCA

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