The liver microsomal FAD-containing monooxygenase. Spectral characterization and kinetic studies.
نویسندگان
چکیده
منابع مشابه
Transient kinetic study of liver microsomal FAD-containing monooxygenase.
Stopped flow kinetic studies have been used to demonstrate three features of the enzymatic mechanism of the microsomal FAD-containing monooxygenase from hog liver. First, in contrast to the bacterial flavin-containing monooxygenases, reduction of the FAD is independent of substrate. Second, the rate of the reaction of reduced enzyme with oxygen to form the C(4a)-peroxyflavin intermediate is ind...
متن کاملThe oxidation of hydrazine derivatives catalyzed by the purified liver microsomal FAD-containing monooxygenase.
A number of hydrazine derivatives were tested as substrates for the purified liver microsomal FAD-containing monooxygenase and the kinetic properties of the oxidation reactions were partially characterized. Only 1,l-dimethylhydrazine, l-methyl-l-phenylhydrazine, and the N-aminoheterocyclic hydrazines are oxidized as effectively as N,N-dimethylaniline, one of the best N-methylamine substrates fo...
متن کاملKinetic characterisation of the FAD dependent monooxygenase TropB and investigation of its biotransformation potential
School, of Chemistry, University of Bristol [email protected] Chemistry of Natural and Microbial Produc Cairo, 12622, Egypt Chemistry Department, Faculty of Science, Arabia Microbiology Department, Faculty of Pharm School of Biochemistry, University of Bristol Institut für Organische Chemie, Leibniz U 30167, Hannover, Germany † Electronic supplementary informa 10.1039/c5ra06693j ‡...
متن کاملMolecular cloning and kinetic characterization of a flavin-containing monooxygenase from Saccharomyces cerevisiae.
An open reading frame from yeast coding for a homologue of flavin containing monooxygenase (FMO) has been cloned into several Escherichia coli expression vectors. A His10 peptide attached to the amino terminus produced a high yield of soluble protein when coexpressed with GroEL and GroES. The protein was purified on an affinity column and characterized. The protein binds one mole per mole of fl...
متن کاملIsolation and Characterization of Rat Liver Microsomal
Microsomal UDP-glucuronosyltransferase activity toward chenodeoxycholic acid and testosterone has been isolated from rat liver and appears to be homogeneous in sodium dodecyl sulfate gel electrophoresis and polyacrylamide gradient gel electrophoresis. The conjugating activities toward chenodeoxycholic acid and testosterone co-purified and showed identical mobilities in disc gel electrophoresis,...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)50388-4