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Literature summary for 1.14.13.8 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
Search for more literature for 1.14.13.8

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Storage Stability

Storage Stability Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
N,N-dimethylaniline + NADPH + O2
-
 Sus scrofa N,N-dimethylaniline N-oxide + NADP+ + H2O
-
 ?
secondary amine + NADPH + O2
-
 Sus scrofa secondary nitrone + NADP+ + H2O first oxidation to the N-hydroxy amine and then to the corresponding nitrone ?
tertiary amine + NADPH + O2
-
 Sus scrofa tertiary N-oxide + NADP+ + H2O
-
 ?

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

Cofactor

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