tsdating ny - Amidating monooxygenase

Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides.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.Once cleaved, a propeptide generally has no independent biological function.

Amidating monooxygenase

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EC production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine αhydroxylating monooxygenase (PHM), 2.

This indicates the type of evidence that supports the existence of the protein.

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peptidylglycine α-amidating enzyme [30]) [28,30]peptide αamidating enzymepeptide αamide synthasepeptide αamide synthetasepeptidyl αamidating enzymepeptidylglycine 2-hydroxylasepeptidylglycine α-amidating mono-oxygenase EC is often called peptidylglycine αamidating monooxygenase (PAM) and the α-amidated product is mentioned as the product of the reaction, but the α-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1.

of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced. This subsection of the ‘Subcellular location’ section describes the extent of a membrane-spanning region of the protein.

It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins. / Processing section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation.

Results showed the following: (1) aggregates of pro ANP and coexpressed pro ANP-EGFP recruited peptidylglycine α-amidating monooxygenase (PAM)-1, an abundant atrial integral vesicle membrane protein; (2) coexpressed N-terminal–mutated (Glu23,24→Gln23,24) and N-terminal–deleted pro ANP-EGFP inhibited recruitment of PAM-1 by up to 60%; (3) 4-phenyl-3-butenoic acid (PBA) (10 μmol/L), a pharmacological inhibitor of the lumenal peptidylglycine α-hydroxylating monooxygenase domain of PAM proteins, inhibited recruitment of endogenous PAM-1 and of coexpressed pro-EGFP–PAM-1; (4) PBA had no effect on exocytosis of the potassium inward rectifier KIR2.1; (5) PBA induced a deformation of the secretory vesicles but did not inhibit docking.

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