EC Number   |
Reaction |
Reference |
|---|
   1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
A copper protein. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. 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. Involved in the biosynthesis of alpha-melanotropin and related biologically active peptides. |
- |
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities, the enzyme possesses 2 catalytic domains |
648703, 657678, 658458 |
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, PHM, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities |
658977 |
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
cleavage of CN bond in N-acetylated glycines, R-CO-NH-CH2-COOH, e.g. found in neuropeptide prohormones |
657649 |
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
detailed analysis of the reaction mechanism, reaction scheme, strictly ordered ping-pong kinetic mechanism in which ascorbate first reduces Cu(II) to Cu(I), semidehydroascorbate being released, after which the peptide binds and finally oxygen, active site structure |
659847 |
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
detailed analysis of the reaction mechanism, role of noncoupled nature of the active site |
658981 |
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
equilibrium ordered mechanism |
438594 |
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
equilibrium ordered mechanism in which substrate binds prior to oxygen |
744361 |
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
equilibrium-ordered and steady-state-random or -ordered reaction mechanism for the wild-type and the mutant Y318F enzyme, respectively, active site Y318 is involved, C-H bond activation is dominated by quantum mechanical tunneling, peptide substrate binding structure at the active site |
657976 |
| 1.14.17.3 | [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
inter-copper electron transfer, interdomain structure |
658976 |
