Autor: |
Lewis, D. F. V., Dickins, M., Weaver, R. J., Eddershaw, P. J., Goldfarb, P. S., Tarbit, M. H. |
Předmět: |
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Zdroj: |
Xenobiotica; Mar1998, Vol. 28 Issue 3, p235-268, 34p |
Abstrakt: |
1. The results of molecular modelling of human CYP2C isozymes, CYP2C9 and CYP2C19, are reported based on an alignment with a bacterial form of the enzyme, CYP102. 2. The three-dimensionalstructures of the CYP2C enzymes are consistent with known experimental evidence from site-directed mutagenesis, antibody recognition and regiospecificity of substrate metabolism. 3. The variations in substrate specificity between CYP2C9 and CYP2C19 can be rationalized in terms of single amino acid residue changes within the putative active site region, of which I99H appears to be the most significant. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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