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Peptidylglycine monooxygenase

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EC number
  
1.14.17.3

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

CAS number
  
90597-47-0

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

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 peptidylglycine 2-hydroxylase, peptidyl alpha-amidating enzyme, peptide-alpha-amide synthetase, synthase, peptide alpha-amide, peptide alpha-amidating enzyme, peptide alpha-amide synthase, peptidylglycine alpha-hydroxylase, peptidylglycine 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.

References

Peptidylglycine monooxygenase Wikipedia