1.14.17.3: peptidylglycine monooxygenase

This is an abbreviated version!
For detailed information about peptidylglycine monooxygenase, go to the full flat file.

Word Map on EC 1.14.17.3

Reaction

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

Synonyms

alpha-AE, bifunctional PAM, bifunctional peptidylglycine alpha-amidating monooxygenase, CG3832, hPHMcc, More, PAM, PAM-1, PAM-2, PAM-A, PAM-B, PAM/PHM, peptide alpha-amidating enzyme, peptide alpha-amide synthase, peptide-alpha-amide synthetase, peptidyl alpha-amidating enzyme, peptidyl alpha-hydroxylating monooxygenase, peptidyl-glycine alpha-amidating monooxygenase, peptidylglycine 2-hydroxylase, peptidylglycine alpha-amidating mono-oxygenase, peptidylglycine alpha-amidating monooxygenase, peptidylglycine alpha-hydroxylase, peptidylglycine alpha-hydroxylating monooxygenase, peptidylglycine alpha-hydroxylating-monooxygenase, peptidylglycine alpha-monooxygenase, peptidylglycine monooxygenase, peptidylglycine-alpha-amidating monooxygenase, PHM, PHMcc, synthase, peptide alpha-amide, type A PAM

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.17.3 peptidylglycine monooxygenase

Metals Ions

Metals Ions on EC 1.14.17.3 - peptidylglycine monooxygenase

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
3.26 mol per mol of bifunctional enzyme
copper
Fe2+
0.37 mol per mol of bifunctional enzyme
Mg2+
0.88 mol per mol of bifunctional enzyme
additional information
-
Ag(I) is iso-electronic with Cu(I) and has been shown to be handled by similar cellular transport processes. Although complexes of Ag in the Ag(III) state exists, the instability of the Ag(II) state renders the metal unsuitable for a functional substitute for copper in enzymes such as PHM. When enzyme mutants H107A/H108A and M109I (a wild-type analogue with both copper sites intact) are incubated with excess AgNO3, each variant binds a single Ag(I) ion, from which it is inferred that Ag(I) binds selectively at the M-center with little or no affinity for the H-center