Characterization of bovine phenol sulfotransferases: evidence of a major role for SULT1B1 in the liver
| Autor: | Kanika V. Choughule, Charles W. Locuson, Michael W.H. Coughtrie |
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| Rok vydání: | 2014 |
| Předmět: |
Male
Gene isoform Sulfotransferase Health Toxicology and Mutagenesis Crystallography X-Ray Toxicology Biochemistry law.invention Nitrophenols Sulfation law Escherichia Animals Humans Pharmacology chemistry.chemical_classification biology Active site General Medicine biology.organism_classification Arylsulfotransferase Amino acid Isoenzymes Liver chemistry biology.protein Recombinant DNA Cattle Female Sulfotransferases Drug metabolism |
| Zdroj: | Xenobiotica. 45:495-502 |
| ISSN: | 1366-5928 0049-8254 |
| Popis: | 1. Cattle are an important component of the human food chain. Drugs used either legally or illegally in cattle may therefore enter the food chain and it is thus important to understand pathways of drug metabolism in this species, including sulfation catalyzed by the sulfotransferases (SULTs).2. In this study, we have analyzed the sulfation of 4-nitrophenol and other compounds in male and female bovine liver and characterized recombinant bovine SULT isoforms 1A1 and 1B1 expressed in Escherichia coli.3. We found that, in contrast to most other mammalian species, the major phenol sulfotransferase SULT1A1 is not expressed in bovine liver. Rather SULT1B1 seems to be a major form in both male and female bovine liver.4. We also identified kinetic differences between bovine and human SULT1A1 and, using the human SULT1A1 crystal structure, identified two amino acid positions in the active site of bovine SULT1A1 (Ile89Val and Phe247Val) that may be responsible for these differences. |
| Databáze: | OpenAIRE |
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