Aldehyde oxidase: Catalysis of the oxidation of N1-methylnicotinamide and pyridoxal
| Autor: | Milan Stanulović, Sterling Chaykin |
|---|---|
| Rok vydání: | 1971 |
| Předmět: |
Male
Niacinamide Aging Chromatography Paper Pyridones Stereochemistry Biophysics Mice Inbred Strains Biology Biochemistry Aldehyde Catalysis Mice chemistry.chemical_compound Sex Factors Inbred strain Oxidoreductase Oxidizing agent Genetics Animals Chemical Precipitation Hepatectomy Molecular Biology Aldehyde oxidase Pyridoxal Alleles Crosses Genetic chemistry.chemical_classification Aldehydes Carbon Isotopes Oxidase test Pyridoxal oxidase activity Rats Kinetics Phenotype Genes Liver chemistry Ammonium Sulfate Picolines Chromatography Gel Female Oxidoreductases Polarography |
| Zdroj: | Archives of Biochemistry and Biophysics. 145:27-34 |
| ISSN: | 0003-9861 |
| Popis: | The oxidation of both N1-methylnicotinamide and pyridoxal appears to be catalyzed by a single liver enzyme, aldehyde oxidase (aldehyde:oxygen oxidoreductase, EC 1.2.3.1). This notion is based on the following evidence: (1) Inbred strains of mice having characteristic and different levels of N1-methylnicotinamide oxidase activity also differ in their abilities to oxidize pyridoxal; the levels of the two activities have been found to vary among the strains in a parallel fashion. (2) The Km values of the N1-methylnicotinamide oxidizing activity for N1-methylnicotinamide and pyridoxal oxidizing activity for pyridoxal also vary among the inbred strains of mice in a parallel fashion. (3) The genetic determinants of pyridoxal and N1-methylnicotinamide oxidizing activity in the mouse do not segregate in the F2 generation or in backcrosses to the parental strains. (4) The levels of N1-methylnicotinamide and pyridoxal oxidizing activities in male mice increase in a parallel fashion upon the attainment of sexual maturity. (5) Competition of N1-methylnicotinamide and pyridoxal for oxidation in vivo has been demonstrated in the rat. (6) The inactivation of N1-methylnicotinamide oxidase activity which is connected with catalytic performance results in an equal loss of pyridoxal oxidase activity. A parallel loss in activity for both substrates also results from the catalysis of pyridoxal oxidation. In the course of these studies, a genetic analysis of aldehyde oxidase in the C58/J and C57B1/6J strains of mice was conducted. The earlier conclusion that aldehyde oxidase is controlled by a single autosomal locus with alleles acting in a codominant manner has been confirmed. |
| Databáze: | OpenAIRE |
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