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Literature summary for 1.14.17.3 extracted from

  • Francisco, W.A.; Blackburn, N.J.; Klinman, J.P.
    Oxygen and hydrogen isotope effects in an active site tyrosine to phenylalanine mutant of peptidylglycine alpha-hydroxylating monooxygenase: mechanistic implications (2003), Biochemistry, 42, 1813-1819.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
Y318F site-directed mutagenesis, active site residue mutant, slightly reduced rate constant for C-H bond cleavage compared to the wild-type enzyme Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
hippuric acid
-
Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information competitive and noncompetitive kinetic isotope effects in wild-type enzyme and mutant Y318F, kinetic mechanism Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ required, reductive activation of Cu(II)-OOH to generate a reactive copper-oxo species Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
[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 Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hippuric acid + ascorbate + O2 C-H bond cleavage is irreversible, protiated and dideuterated substrate Rattus norvegicus ? + dehydroascorbate + H2O
-
ir
peptidylglycine + ascorbate + O2 C-H bond cleavage is irreversible, activation of molecular O2 and of the C-H bond of the substrate, mechanism, reductive activation of Cu(II)-OOH to generate a reactive copper-oxo species Rattus norvegicus peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
ir

Synonyms

Synonyms Comment Organism
peptidylglycine alpha-hydroxylating monooxygenase
-
Rattus norvegicus
PHM
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information intrinsic rate constants for wild-type and mutant Y318F enzyme Rattus norvegicus
13.6
-
hippuric acid pH 6.0, 37°C, [2H2]-hippuric acid, mutant Y318F Rattus norvegicus
25
-
hippuric acid pH 6.0, 37°C, [2H2]-hippuric acid, wild-type enzyme Rattus norvegicus
27.6
-
hippuric acid pH 6.0, 37°C, [1H2]-hippuric acid, mutant Y318F Rattus norvegicus
39.1
-
hippuric acid pH 6.0, 37°C, [1H2]-hippuric acid, wild-type enzyme Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
Rattus norvegicus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.9
-
hippuric acid pH 6.0, 37°C, [1H2]-hippuric acid, wild-type enzyme Rattus norvegicus
4.5
-
hippuric acid pH 6.0, 37°C, [2H2]-hippuric acid, wild-type enzyme Rattus norvegicus
7
-
hippuric acid pH 6.0, 37°C, [2H2]-hippuric acid, mutant Y318F Rattus norvegicus
22
-
hippuric acid pH 6.0, 37°C, [1H2]-hippuric acid, mutant Y318F Rattus norvegicus