Alpha amidating enzyme

23-Sep-2017 10:39

The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part.

Background: Peptidylglycine alpha-Amidating Monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important post-translational modification.The protein contains two enzymes, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL), that act sequentially to catalyse the alpha-amidation of neuroendocrine peptides [PMID: 1988445, PMID: 1448112]: The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide.The first step of the reaction is catalysed by peptidylglycine alpha-hydroxylating monooxygenase (PHM), and is dependent on copper, ascorbate and molecular oxygen; peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) catalyses the second step of the reaction [PMID: 1448112].All of the histidine and methionine residues involved in coordinating the two catalytic copper ions are conserved in all known PHM sequences.

Interestingly, all the spectral and crystallography data indicate that the two copper ions are farther apart than expected for a reaction requiring both copper ions to undergo a reduction–oxidation cycle.Results: Modification-specific antibodies reveal that peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia.

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