Conformational heterogeneity suggests multiple substrate binding modes in CYP106A2.

ABSTRACT: CYP106A2 (cytochrome P450_meg) is a bacterial enzyme originally isolated from B. megaterium, and has been shown to hydroxylate a wide variety of substrates, including steroids. The regio- and stereochemistry of CYP106A2 hydroxylation has been shown to be dependent on a variety of factors, and hydroxylation often occurs at more than one site and/or with lack of stereospecificity for some substrates. Comprehensive backbone ¹⁵N, ¹H and ¹³C resonance assignments based on multidimensional nuclear magnetic resonance (NMR) experiments performed with uniform and selective isotopically labeled CYP106A2 samples are reported herein, and broadening and splitting of resonances assigned to regions of the enzyme shown to be affected by substrate binding in other

SUBMITTER: Wong NR 

PROVIDER: S-EPMC9992128 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature