[The interaction of organophosphorus amino acid analogs with cytochrome P-450 2B4].
Substance Nomenclature: | 0 (Amino Acids) 0 (Organophosphorus Compounds) 53-59-8 (NADP) 9035-51-2 (Cytochrome P-450 Enzyme System) EC 1.14.- (Steroid Hydroxylases) EC 1.14.14.1 (Aryl Hydrocarbon Hydroxylases) EC 1.14.14.1 (steroid 15-alpha-hydroxylase) YQE403BP4D (Phenobarbital) |
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Entry Date(s): | Date Created: 19961101 Date Completed: 19970305 Latest Revision: 20161020 |
Update Code: | 20240829 |
PMID: | 9044681 |
Autor: | Shumiantseva VV, Meshkov SV, Uvarov VIu, Archakov AI |
Jazyk: | ruština |
Zdroj: | Izvestiia Akademii nauk. Seriia biologicheskaia [Izv Akad Nauk Ser Biol] 1996 Nov-Dec (6), pp. 749-53. |
Abstrakt: | Interaction between phosphorus amino acids analogs, 1-aminoalkylphosphonous and 1-aminoalkylthiophosphonic acids, and microsomes from the liver of phenobarbital-induced rabbits was studied. The phosphorus amino acids analogs cause type I and reverse type I spectral changes, respectively. A new reaction in the microsomal monooxygenase system was revealed. In the presence of NADPH, 1-aminoalkylphosphonous acids can be transformed to the corresponding 1-aminoalkylphosphonic acids by the reaction P-H-->P-OH. The reaction was monitored by 1H-NMR spectroscopy. 1-Aminoalkylphosphonous acids also serve as substrates for the NADPH-dependent monooxygenase system. 31P-NMR has shown that the oxidative desulfuration produces 1-aminoalkylphosphonous acids according to the reaction P=S-->P=O. Neither 1-aminoalkylphosphonous nor 1-aminoalkylphosphonic acids are deaminated in the NADPH-dependent monooxygenase system as follows from 1H-NMR spectroscopy. |
Databáze: | MEDLINE |
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