Exploring the molecular basis for substrate specificity in homologous macrolide biosynthetic cytochromes P450.

ABSTRACT: Cytochromes P450 (P450s) are nature's catalysts of choice for performing demanding and physiologically vital oxidation reactions. Biochemical characterization of these enzymes over the past decades has provided detailed mechanistic insight and highlighted the diversity of substrates P450s accommodate and the spectrum of oxidative transformations they catalyze. Previously, we discovered that the bacterial P450 MycCI from the mycinamicin biosynthetic pathway in Micromonospora griseorubida possesses an unusually broad substrate scope, whereas the homologous P450 from tylosin-producing Streptomyces fradiae (TylHI) exhibits a high degree of specificity for its native substrate. Here, using biochemical, structural, and computational approaches, we aimed to understand the molecular

SUBMITTER: DeMars MD 

PROVIDER: S-EPMC6827315 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature