Peptidylglycine alpha amidating

Peptidylglycine alpha amidating

Recent attention has been focused on the reactive intermediates generated at the mononuclear copper active sites of copper monooxygenases such as dopamine β-monooxygenase (DβM), tyramine β-monooxygenase (TβM), peptidylglycine-α-hydroxylating monooxygenase (PHM), and polysaccharide monooxygenases (PMO).

To reveal the roles of phenylalanine ammonia-lyase (PAL) in low temperature tolerance in cucumber seedlings, a specific PAL inhibitor (AOPP) was sprayed to the seedlings, and then the stress tolerance was determined.

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Bulleted lists, for instance, were only used because it is impossible to automatically integrate independent facts into a continuous text.

It has two enzymatically active domains with catalytic activities - peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL).

Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene, but some of their full-length sequences are not yet known., this process relies on a copper cofactor.

Peptidyl-glycine alpha-amidating monooxygenase is an enzyme that is required for the biosynthesis of many signaling peptides.

This transformation is achieved by conversion of a prohormone to the corresponding amide (C(O)NHThis gene encodes a multifunctional protein.

The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC 4.3.2.5 peptidylamidoglycolate lyase.PAM possesses two enzymatic activities on a single polypeptide chain (2), due to the presence of a peptidylglycine alpha ‑hydroxylating monooxygenase (PHM) domain and a peptidyl‑ alpha ‑hydroxyglycine alpha ‑amidating lyase (PAL) domain.The C-terminal glycines of precursor peptides are hydroxylated at the glycine alpha carbon by the PHM activity in a reaction that requires ascorbate, then the PAL activity completes the amidation, releasing glyoxylate in the process.Much of the current information on this page has been automatically compiled from Pubmed.This transformation is achieved by conversion of a prohormone to the corresponding amide (C(O)NH This gene encodes a multifunctional protein.

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Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme.

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