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Proteomics, modeling, and fluorescence assays delineate cytochrome b₅ residues involved in binding and stimulation of cytochrome P450 17A1 17,20-lyase.

ABSTRACT: Cytochrome b₅ (b₅) is known to stimulate some catalytic activities of cytochrome P450 (P450, CYP) enzymes, although mechanisms still need to be defined. The reactions most strongly enhanced by b₅ are the 17,20-lyase reactions of P450 17A1 involved in steroid biosynthesis. We had previously used a fluorescently labeled human b₅ variant (Alexa 488-T70C-b₅) to characterize human P450 17A1-b₅ interactions, but subsequent proteomic analyses indicated that lysines in b₅ were also modified with Alexa 488 maleimide in addition to Cys-70, due to disulfide dimerization of the T70C mutant. A series of b₅ variants were constructed with Cys replacements for the identified lysine residues and labeled with the dye. Fl

SUBMITTER: Tateishi Y

PROVIDER: S-EPMC10878793 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature

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Proteomics, modeling, and fluorescence assays delineate cytochrome b₅ residues involved in binding and stimulation of cytochrome P450 17A1 17,20-lyase.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Proteomics, modeling, and fluorescence assays delineate cytochrome b5 residues involved in binding and stimulation of cytochrome P450 17A1 17,20-lyase.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Proteomics, modeling, and fluorescence assays delineate cytochrome b₅ residues involved in binding and stimulation of cytochrome P450 17A1 17,20-lyase.