This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3mig
From Proteopedia
| Line 1: | Line 1: | ||
| - | {{Seed}} | ||
| - | [[Image:3mig.jpg|left|200px]] | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_3mig", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_3mig| PDB=3mig | SCENE= }} | {{STRUCTURE_3mig| PDB=3mig | SCENE= }} | ||
| - | |||
===Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate=== | ===Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate=== | ||
| + | {{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. | |
| - | + | ||
| - | + | ||
| - | - | + | |
| - | + | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3mig]] 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=3MIG OCA]. | |
==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]] | ||
| Line 34: | Line 21: | ||
[[Category: Monooxygenase]] | [[Category: Monooxygenase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 24 14:15:09 2010'' | ||
Revision as of 20:56, 17 April 2013
Contents |
Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate
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
3mig 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
