Peptidylglycine alpha amidating enzyme
Ideally this entry shall become one comprehensive and continuous article.Bulleted lists, for instance, were only used because it is impossible to automatically integrate independent facts into a continuous text.Conclusion: PAM-dependent amidation has the potential to signal oxygen levels in the same range as the hypoxia-inducible factor (HIF) system.Significance: Physiological effects of hypoxia may be PAM-dependent.This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed. Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. 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].
Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’. This subsection of the ‘Names and taxonomy’ section contains the taxonomic hierarchical classification lineage of the source organism.
Interactions between biological pathways and molecular oxygen require robust mechanisms for detecting and responding to changes in cellular oxygen availability, in order to support oxygen homeostasis.
Peptidyl glycine alpha-amidating monooxygenase (PAM) catalyzes a two-step reaction resulting in the C-terminal amidation of peptides, a process important for their stability and biological activity.
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.
Once cleaved, a propeptide generally has no independent biological function.
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