1phm
From Proteopedia
(New page: 200px<br /> <applet load="1phm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1phm, resolution 1.90Å" /> '''PEPTIDYLGLYCINE ALP...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1PHM is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with CU, AZI and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PHM OCA]]. | + | 1PHM is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with CU, AZI and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3]]. Structure known Active Site: CUB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PHM OCA]]. |
==Reference== | ==Reference== | ||
Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Science. 1997 Nov 14;278(5341):1300-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9360928 9360928] | Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Science. 1997 Nov 14;278(5341):1300-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9360928 9360928] | ||
| + | [[Category: Peptidylglycine monooxygenase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:00:34 2007'' |
Revision as of 09:55, 30 October 2007
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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 ... [(full description)]
About this Structure
1PHM is a [Single protein] structure of sequence from [Rattus norvegicus] with CU, AZI and GOL as [ligands]. Active as [Peptidylglycine monooxygenase], with EC number [1.14.17.3]. Structure known Active Site: CUB. Full crystallographic information is available from [OCA].
Reference
Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Science. 1997 Nov 14;278(5341):1300-5. PMID:9360928
Page seeded by OCA on Tue Oct 30 12:00:34 2007
