Structural modeling of cytochrome P450 51 from a deep-sea fish points to a novel structural feature in other CYP51s.

ABSTRACT: Cytochromes P450 (CYP), enzymes involved in the metabolism of endogenous and xenobiotic substrates, provide an excellent model system to study how membrane proteins with unique functions have catalytically adapted through evolution. Molecular adaptation of deep-sea proteins to high hydrostatic pressure remains poorly understood. Herein, we have characterized recombinant cytochrome P450 sterol 14α-demethylase (CYP51), an essential enzyme of cholesterol biosynthesis, from an abyssal fish species, Coryphaenoides armatus. C. armatus CYP51 was heterologously expressed in Escherichia coli following N-terminal truncation and purified to homogeneity. Recombinant C. armatus CYP51 bound its sterol substrate lanosterol giving a Type I binding spectra (K_D 15 μM) and catalyzed lanosterol 14α

SUBMITTER: Goldstone JV 

PROVIDER: S-EPMC10330650 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature