Alpha amidating enzyme


02-Mar-2020 03:15

The catalytic core of PHM consists of two β-clamshell or sandwich domains.Each approximately 150-amino acid domain contains a single copper binding site. The two domains are held together by a single hydrophilic linker strand, whereas the interiors of the domains are very hydrophobic.Results: Modification-specific antibodies reveal that peptide substrate amidation is strikingly sensitive to the exposure of cells to moderate hypoxia.Conclusion: PAM-dependent amidation has the potential to signal oxygen levels in the same range as the hypoxia-inducible factor (HIF) system.Interestingly, in Drosophila, the PHM and PAL enzyme are not fused.The Drosophila genome predicts expression of one monofunctional PHM gene and two monofunctional PAL genes [PMID: 15198673].Elimination of the exon encoding the transmembrane domain yields a soluble, secreted enzyme.Elimination of the flexible linker region between PHM and PAL (exon 16) greatly reduces the ability of cells to separate the two catalytic activities.

Background: Peptidylglycine alpha-Amidating Monooxygenase (PAM) is solely responsible for catalysis of amidation, a biologically important post-translational modification.wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound Welcome!If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text.Different amidation events on chromogranin A, and on peptides processed from proopiomelanocortin, manifest similar striking sensitivity to hypoxia in a range of neuroendocrine cells, being progressively inhibited from mild (7% O2) to severe (1% O2) hypoxia.

In developing Drosophila melanogaster larvae, FMRF amidation in thoracic ventral (Tv) neurons is strikingly suppressed by hypoxia.

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.



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