Functional characterization and unraveling the structural determinants of novel steroid hydroxylase CYP154C7 from Streptomyces sp. PAMC26508.

ABSTRACT: This study characterized cytochrome P450 enzyme CYP154C7 from Streptomyces sp. PAMC26508, emphasizing its capability to hydroxylate steroids, especially at the 16α-position. The enzymatic assay of CYP154C7 demonstrated effective conversion across a pH range of 7.2-7.6, with optimal activity at 30 °C in the Pdx/PdR plus NADH system. Kinetic analysis on most converted steroids (androstenedione and adrenosterone) was performed which shows a greater affinity for androstenedione (K _m , 11.06 ± 1.903 μM; V _max, 0.0062 ± 0.0002 sec^-1) compared to adrenosterone (K _m , 34.50 ± 6.2 μM; V _max, 0.0119 ± 0.0007 sec^-1). A whole-cell system in Escherichia coli, overexpressing recombin

SUBMITTER: Paudel P 

PROVIDER: S-EPMC11544072 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature