Mechanism of biochemical action of substituted 4-Methylbenzopyran-2-ones. Part 6: hydrolysis of 7,8-diacetoxy-4-methylcoumarin by a novel deacetylase in rat liver microsomes — a simple method for assay and characterisation
| Autor: | Hanumantha Rao G Raj, Subhash C. Jain, Virinder S. Parmar, Sunil K. Sharma, Yogesh K Tyagi, Jesper Wengel, Sanjay Goel, Carl Erik Olsen |
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| Rok vydání: | 2000 |
| Předmět: |
Male
Stereochemistry Clinical Biochemistry Kinetics Pharmaceutical Science Biochemistry Substrate Specificity Hydrolysis Coumarins Drug Discovery Animals Benzopyrans Rats Wistar Molecular Biology chemistry.chemical_classification biology Chemistry Organic Chemistry Substrate (chemistry) Hydrogen-Ion Concentration Enzyme assay Rats Enzyme Acetylation Microsomes Liver biology.protein Microsome Molecular Medicine Acetylesterase Carboxylic Ester Hydrolases Deacetylase activity |
| Zdroj: | Bioorganic & Medicinal Chemistry. 8:233-237 |
| ISSN: | 0968-0896 |
| DOI: | 10.1016/s0968-0896(99)00272-2 |
| Popis: | The existence of a novel microsomal deacetylase in rat liver catalysing deacetylation of diacetoxy 4-methylcoumarins has been reported. A simple method is outlined for the enzyme assay based upon the quantification of the dihydroxy derivative by measuring the UV absorption of its complex with ADP and Fe 3+ at 600 nm. The enzyme can be routinely assayed using 7,8-diacetoxy-4-methylcoumarin (DAMC) as the substrate and demonstrated hyperbolic kinetics and yielded K m and ν max values of 1250 μM and 500 units, respectively. The pH optima was found to be 7.5 for the enzyme. No DAMC deacetylase activity was found in hepatic cytosol and the enzyme activity was not discernible in extrahepatic tissues. |
| Databáze: | OpenAIRE |
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