Peptidylglycine monooxygenase

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peptidylglycine monooxygenase
Identifiers
EC no. 1.14.17.3
CAS no. 90597-47-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PMC articles
PubMed articles
NCBI proteins

In enzymology, a peptidylglycine monooxygenase (EC 1.14.17.3) is an enzyme that catalyzes the chemical reaction

peptidylglycine + ascorbate + O2 peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O

The 3 substrates of this enzyme are peptidylglycine, ascorbate, and O2, whereas its 3 products are peptidyl(2-hydroxyglycine), dehydroascorbate, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 2-hydroxylase, alpha-amidating enzyme, peptide-alpha-amide synthetase, synthase, peptide alpha-amide, peptide alpha-amidating enzyme, peptide alpha-amide synthase, alpha-hydroxylase, alpha-amidating monooxygenase, PAM-A, PAM-B, and PAM. It employs one cofactor, copper.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1OPM, 1PHM, 1SDW, 1YI9, 1YIP, 1YJK, 1YJL, and 3PHM.

Related Research Articles

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<span class="mw-page-title-main">Peptidylglycine alpha-amidating monooxygenase</span> Protein-coding gene in the species Homo sapiens

Peptidyl-glycine alpha-amidating monooxygenase, or PAM, is an enzyme that catalyzes the conversion of an n+1 residue long peptide with a C-terminal glycine into an n-residue peptide with a terminal amide group. In the process, one molecule of O2 is consumed and the glycine residue is removed from the peptide and converted to glyoxylic acid.

<span class="mw-page-title-main">Amidorphin</span> Chemical compound

Amidorphin is an endogenous, C-terminally amidated, opioid peptide generated as a cleavage product of proenkephalin A in some mammalian species; in humans and most other species, the peptide is 1 residue longer and is not amidated. Amidorphin is widely distributed in the mammalian brain, with particularly high concentrations found in the striatum, and outside of the brain in adrenal medulla and posterior pituitary. The 26-residue peptide named amidorphin is found in several species including bovine, sheep, and pig. Humans and commonly studied lab animals produce a 27-residue peptide that does not have an amidated C-terminal residue; this is due to the absence of a Gly in the precursor sequence and replacement with Ala, which is not a substrate for the amidating enzyme. The properties of the 27-residue peptide are presumably similar to those of amidorphin, although this has not been adequately tested.

<span class="mw-page-title-main">Monooxygenase DBH-like 1</span> Protein-coding gene in the species Homo sapiens

DBH-like monooxygenase protein 1, also known as monooxygenase X, is an enzyme that in humans is encoded by the MOXD1 gene.

<span class="mw-page-title-main">Copper type II ascorbate-dependent monooxygenase</span> Class of enzymes

In molecular biology, the copper type II ascorbate-dependent monooxygenases are a class of enzymes that require copper as a cofactor and which use ascorbate as an electron donor. This family contains two related enzymes, dopamine beta-monooxygenase EC 1.14.17.1 and peptidylglycine alpha-amidating monooxygenase EC 1.14.17.3. There are a few regions of sequence similarities between these two enzymes, two of these regions contain clusters of conserved histidine residues which are most probably involved in binding copper.

References


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