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Literature summary extracted from

  • Francisco, W.A.; Knapp, M.J.; Blackburn, N.J.; Klinman, J.P.
    Hydrogen tunneling in peptidylglycine alpha-hydroxylating monooxygenase (2002), J. Am. Chem. Soc., 124, 8194-8195.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.17.3 Cu2+
-
 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
1.14.17.3 Rattus norvegicus
-
 bifunctional alpha-AE
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.17.3 medullary thyroid carcinoma cell
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.17.3 hippuric acid + ascorbate + O2 i.e. N-benzoylglycine Rattus norvegicus alpha-hydroxyhippuric acid + dehydroascorbate + H2O
-
 ?
1.14.17.3 additional information cleavage of C-H bond in the second reaction step is irreversible Rattus norvegicus ?
-
 ?
1.14.17.3 additional information tunneling of hydrogen ion, relatively flexible Rattus norvegicus ?
-
 ?
1.14.17.3 peptidylglycine + ascorbate + O2
-
 Rattus norvegicus peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.17.3 additional information
-
 above 40°C, temperature dependence Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.17.3 3
-
 N-benzoylglycine 15°C Rattus norvegicus
1.14.17.3 14.5
-
 N-benzoylglycine 37°C Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.17.3 ascorbate
-
 Rattus norvegicus