1phm: Difference between revisions

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[[Image:1phm.~~jpg~~|left|200px]]

[[Image:1phm.png|left|200px]]

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~~'''~~PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT~~'''~~

===PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT===

~~==Overview==~~

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Many neuropeptides and peptide hormones require amidation at the carboxyl terminus for activity. Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the amidation of these diverse physiological regulators. The amino-~~terminal domain of the bifunctional PAM protein is a peptidylglycine alpha~~-~~hydroxylating monooxygenase (PHM) with two coppers that cycle through cupric and cuprous oxidation states.~~ The ~~anomalous signal of~~ the ~~endogenous coppers was used~~ to ~~determine~~ the ~~structure of~~ the ~~catalytic core of oxidized rat PHM with and without bound peptide substrate~~. ~~These structures strongly suggest that the PHM reaction proceeds via activation of substrate by a copper~~-~~bound oxygen species. The mechanistic and structural insight gained from the PHM structures can be directly extended to dopamine beta~~-~~monooxygenase.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9360928}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9360928 is the PubMed ID number.

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==About this Structure==

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[[Category: Monooxygenase]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 05~~:05:41 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:39:13 2008''

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-[[Image:1phm.jpg|left|200px]]
+{{Seed}}
+[[Image:1phm.png|left|200px]]
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 {{STRUCTURE_1phm|  PDB=1phm  |  SCENE=  }}
-'''PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT'''
+===PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT===
-==Overview==
+<!--
-Many neuropeptides and peptide hormones require amidation at the carboxyl terminus for activity. Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the amidation of these diverse physiological regulators. The amino-terminal domain of the bifunctional PAM protein is a peptidylglycine alpha-hydroxylating monooxygenase (PHM) with two coppers that cycle through cupric and cuprous oxidation states. The anomalous signal of the endogenous coppers was used to determine the structure of the catalytic core of oxidized rat PHM with and without bound peptide substrate. These structures strongly suggest that the PHM reaction proceeds via activation of substrate by a copper-bound oxygen species. The mechanistic and structural insight gained from the PHM structures can be directly extended to dopamine beta-monooxygenase.
+The line below this paragraph, {{ABSTRACT_PUBMED_9360928}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9360928 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9360928}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Monooxygenase]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:05:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:39:13 2008''