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Identification of selectivity‐determining residues in cytochrome P450 monooxygenases: A systematic analysis of the substrate recognition site 5 by Alexander Seifert; Jürgen Pleiss is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The large and diverse family of cytochrome P450 monooxygenases (CYPs) was systematically analyzed to identify selectivity‐ and specificity‐determining residues in the substrate recognition site 5, which is located in close vicinity to the heme center. A positively charged heme‐interacting residue was identified in the structures of 29 monooxygenases and in 97.7% of the 6379 CYP sequences investigated here. This heme‐interacting residue restricts the conformation of the substrate recognition site 5 and is preferentially located at position 10 or 11 after the conserved ExxR motif (in 94.4% of the sequences), in 3.3% of the sequences at position 9 or 12. As a result, a classification by the position of the heme‐interacting residue allows to predict residues that are closest to the heme center and restrict its accessibility. In 98.4% of all CYP sequences a preferentially hydrophobic residue is located at position 5 after the ExxR motif that is predicted to point close to the heme center. Replacing this residue by hydrophobic residues of different size has been shown to change substrate specificity and regioselectivity for CYPs of different superfamilies. Twenty‐seven percen

Who reads Identification of selectivity‐determining residues in cytochrome P450 monooxygenases: A systematic analysis of the substrate recognition site 5?

Author

Alexander Seifert; Jürgen Pleiss

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2008

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)