Although both bacterial CYP102 (P450BM3) and mammalian CYP4A isozymes share a common function as fatty acid hydroxylases, distinctly different preferred sites of oxidation are observed with the CYP102 performing the usual non-terminal hydroxylation or epoxidation and the CYP4A enzymes performing the
HOMOLOGY MODELING AND SUBSTRATE BINDING STUDY OF HUMAN KYNURENINE AMINOTRANSFERASE III
โ Scribed by XU, YU; ZHENG, QING-CHUAN; ZHANG, HONG-XING; SUN, CHIA-CHUNG
- Book ID
- 120509675
- Publisher
- World Scientific Publishing Company
- Year
- 2012
- Tongue
- English
- Weight
- 409 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0219-6336
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It is well established that the variable binding-site architecture and composition of the P450 metabolizing heme proteins are major modulators of substrate and product specificity. Even the three closely related human liver isozymes, CYP2C9, CYP2C18, and CYP2C19, do not share all substrates and do n