Structural and Kinetic Basis of Steroid 17α,20-Lyase Activity in Teleost Fish Cytochrome P450 17A1 and Its Absence in Cytochrome P450 17A2

• Published in: The Journal of biological chemistry Vol. 290; no. 6; pp. 3248 - 3268
• Main Authors: Pallan, Pradeep S., Nagy, Leslie D., Lei, Li, Gonzalez, Eric, Kramlinger, Valerie M., Azumaya, Caleigh M., Wawrzak, Zdzislaw, Waterman, Michael R., Guengerich, F. Peter, Egli, Martin
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 06.02.2015; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Androstenes - pharmacology; Animals; Catalytic Domain; Cytochrome P450; Enzyme Kinetics; Enzymology; Kinetics; Molecular Docking Simulation; Molecular Sequence Data; Pre-steady-state Kinetics; Progesterone - pharmacology; Protein Binding; Steroid 17-alpha-Hydroxylase - antagonists & inhibitors; Steroid 17-alpha-Hydroxylase - chemistry; Steroid 17-alpha-Hydroxylase - metabolism; Steroidogenesis; X-ray Crystallography; Zebrafish; Zebrafish Proteins - antagonists & inhibitors; Zebrafish Proteins - chemistry; Zebrafish Proteins - metabolism; Steroidogenesis; Enzyme Kinetics; Pre-steady-state Kinetics; X-ray Crystallography; Cytochrome P450

Cytochrome P450 (P450) 17A enzymes play a critical role in the oxidation of the steroids progesterone (Prog) and pregnenolone (Preg) to glucocorticoids and androgens. In mammals, a single enzyme, P450 17A1, catalyzes both 17α-hydroxylation and a subsequent 17α,20-lyase reaction with both Prog and Pr...