Peptidylglycine amidating monooxygenase

Posted by / 20-Oct-2017 04:23

The catalytic core of PHM was defined using controlled protease digestion, and its structure was explored by assigning disulfides, examining site-directed mutants, and employing spectroscopy and X-ray crystallography.The catalytic core of PHM consists of two β-clamshell or sandwich domains.Its functional role has been studied using enzyme inhibitors.Thus selective, peripheral PAM inhibition reduces substance P along with an anti-inflammatory action.4. Peptidylglycine α-amidating mono-oxygenase (PAM) is a bifunctional key enzyme in the bioactivation of neuropeptides.

In vertebrates, peptidylglycine alpha-amidating monooxygenase (PAM) is a multifunctional protein found in secretory granules.Peptidylglycine α-amidating mono-oxygenase (PAM) is a bifunctional key enzyme in the bioactivation of neuropeptides.Peptidylglycine alpha-amidating monooxygenase (EC 1.14.17.3) is a multifunctional protein containing 2 enzymes, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL), that act sequentially to catalyze the alpha-amidation of neuroendocrine peptides. Peptidylglycine alpha-amidating monooxygenase (EC 1.14.17.3) is a multifunctional protein containing 2 enzymes, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL), that act sequentially to catalyze the alpha-amidation of neuroendocrine peptides. (1990) showed that alternative splicing generates 2 forms of PAM m RNA in humans. (1993) used Southern blot analysis of human placental DNA to demonstrate that PAM is encoded by a single gene. (1992) mapped the human PAM gene to the long arm of chromosome 5. Peptidylglycine α-amidating monooxygenase (PAM) catalyzes the amidation of these diverse physiological regulators.The amino-terminal domain of the bifunctional PAM protein is a peptidylglycine α-hydroxylating monooxygenase (PHM) with two coppers that cycle through cupric and cuprous oxidation states.

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