1phm
From Proteopedia
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Revision as of 13:54, 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
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