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Literature summary extracted from

  • Poulsen, L.L.; Sofer, S.S.; Ziegler, D.M.
    Properties and applications of an immobilized mixed-function hepatic drug oxidase (1976), Methods Enzymol., 44, 849-856.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.8 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.8 liver
-
Sus scrofa
-

Storage Stability

EC Number Storage Stability Organism
1.14.13.8 glass-bead immobilized enzyme: 0-4°C, 0.025 M phosphate buffer, several months with little or no loss of activity Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.8 additional information catalyzes NADPH- and O2-dependent N-oxidation of N-substituted amines and hydrazines and the S-oxidation of thioureylenes and thiols Sus scrofa ?
-
?
1.14.13.8 N,N-dimethylaniline + NADPH + O2
-
Sus scrofa N,N-dimethylaniline N-oxide + NADP+ + H2O
-
?
1.14.13.8 secondary amine + NADPH + O2
-
Sus scrofa secondary nitrone + NADP+ + H2O first oxidation to the N-hydroxy amine and then to the corresponding nitrone ?
1.14.13.8 tertiary amine + NADPH + O2
-
Sus scrofa tertiary N-oxide + NADP+ + H2O
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.8 25 28 N,N-dimethylaniline, immobilized enzyme Sus scrofa

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.14.13.8 38
-
pH 7.6, half-life of free enzyme: 10 min, half-life of immobilized enzyme 5 h Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.8 7.6
-
N,N-dimethylaniline, immobilized enzyme Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.8 NADH concentration of NADPH required for half-maximal velocity is one-tenth of that for NADH Sus scrofa
1.14.13.8 NADPH
-
Sus scrofa