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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
mechanism
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
mechanism
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
mechanism
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
sequential activity of 2 enzymes contained within a bifunctional protein
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
equilibrium ordered mechanism
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
kinetic model for slow-binding inhibition
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
structural analysis of mutant H172A, binding of ligands CO, Cu2+
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
structural analysis
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
ping-pong-mechanism
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
structure analysis
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[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.
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
kinetic analysis
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[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
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[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
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[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
[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
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[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
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[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
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[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
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[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
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
inter-copper electron transfer, interdomain structure
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
mechanism, substrate binding structure
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[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
equilibrium ordered mechanism in which substrate binds prior to oxygen
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
reaction mechanism simulation using quantum mechanics/molecular mechanics calculations, molecular dynamics simulations, and the enzyme crystal structure, PDB 1SDW, detailed overview. The overall reaction of PHM consists of a stereospecific hydroxylation of the pro-S hydrogen using molecular O2 as oxygen source. Two electrons and two protons are consumed during the reaction. Ascorbate is the best (but not the only possible) reductant. In the protein resting state, both copper atoms are in the +2 oxidation state and are reduced by ascorbate to +1. Molecular oxygen then binds to CuM as the substrate binds to the protein. first and rate-limiting step is hydrogen abstraction, second step is OH rebinding via double protonated intermediate and transition state (TS2)
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O
stopped-flow studies of the reduction of the copper centers suggest a bifurcated electron transfer pathway in peptidylglycine monooxygenase