Peptidylglycine alpha amidating enzyme
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It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first. This subsection of the “Names and Taxonomy” section is present for entries that are part of a proteome, i.e.
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.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].PHM share protein sequence similarity with dopamine-beta-monooxygenases (DBH), a class of ascorbate-dependent enzymes that requires copper as a cofactor and uses ascorbate as an electron donor.PHM and DBH share a few regions of sequence similarity, some of which contain clusters of conserved histidine residues that may be involved in copper binding [PMID: 11028916, PMID: 16301310].Here we show that in human, mouse and insect cells, peptide amidation is exquisitely sensitive to hypoxia.
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.
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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.
C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
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