1phm: Difference between revisions

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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9360928 (full description)]]

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]].  

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