Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding

Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding

Enzymatic alkane hydroxylation reactions are useful for producing pharmaceutical and agricultural chemical intermediates from hydrocarbons. Several cytochrome P450 enzymes catalyze the regio- and stereo-specific hydroxylation of alkanes. We evaluated the substrate binding of a putative CYP alkane hy...

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Bibliographic Details
Main Authors: Chang Woo Lee, Sang-Cheol Yu, Joo-Ho Lee, Sun-Ha Park, Hyun Park, Tae-Jin Oh, Jun Hyuck Lee
Format: Article
Language:English
Published: MDPI AG 2016-12-01
Series:International Journal of Molecular Sciences
Subjects:
cytochrome P450
substrate binding assay
crystal structure
Sphingomonas sp.
X-ray crystallography
Online Access:http://www.mdpi.com/1422-0067/17/12/2067

Internet

http://www.mdpi.com/1422-0067/17/12/2067

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