Khaled S. Al Salhen
Role of Fish Hepatic Aldehyde Oxidase in Oxidative in vitro Metabolism of Phenanthridine Heterocyclic Aromatic Compound
206 - 211
2014
8
3
International Journal of Chemical and Molecular Engineering
https://publications.waset.org/pdf/9997664
https://publications.waset.org/vol/87
World Academy of Science, Engineering and Technology
Aldehyde oxidase is molybdoflavoenzyme involved in the oxidation of hundreds of endogenous and exogenous and Nheterocyclic compounds and environmental pollutants. Uncharged Nheterocyclic aromatic compounds such phenanthridine are commonly distributed pollutants in soil, air, sediments, surface water and groundwater, and in animal and plant tissues. Phenanthridine as uncharged Nheterocyclic aromatic compound was incubated with partially purified aldehyde oxidase from rainbow trout fish liver. Reversedphase HLPC method was used to separate the oxidation products from phenanthridine and the metabolite was identified. The 6(5H)phenanthridinone was identified the major metabolite by partially purified aldehyde oxidase from fish liver. Kinetic constant for the oxidation reactions were determined spectrophotometrically and showed that this substrate has a good affinity (Km 78 ± 7.6µM) for hepatic aldehyde oxidase, will be a significant pathway. This study confirms that partially purified aldehyde oxidase from fish liver is indeed the enzyme responsible for the in vitro production 6(5H)phenanthridinone metabolite as it is a major metabolite by mammalian aldehyde oxidase, coupled with a relatively high oxidation rate (0.77± 0.03 nmolminmg protein). In addition, the kinetic parameters of hepatic fish aldehyde oxidase towards the phenanthridine substrate indicate that in vitro biotransformation by hepatic fish aldehyde oxidase will be a significant pathway. This study confirms that partially purified aldehyde oxidase from fish liver is indeed the enzyme responsible for the in vitro production 6(5H)phenanthridinone metabolite as it is a major metabolite by mammalian aldehyde oxidase.
Open Science Index 87, 2014