Isolation of two distinct cytochromes P-45011 beta with aldosterone synthase activity from bovine adrenocortical mitochondria.
Two distinct forms of cytochrome P-45011 beta, with apparent molecular weights of 48,500 (48.5K) and 49,500 (49.5K), have been isolated from bovine adrenocortical mitochondria. Their amino acid sequences up to the 19th position from the N-terminus were only different at the 6th position (Val and Ala for the 48.5K and 49.5K enzymes, respectively). Each sequence was assignable to a distinct cDNA clone for cytochrome P-450(11) beta (Kirita, S., et al. [1988] J. Biochem. 104, 683-686), indicating that the two proteins originate from different genes in bovine adrenocortical cells. Both forms of cytochrome P-450(11) beta were capable of catalyzing aldosterone synthesis as well as the 11 beta- and 18-hydroxylation of 11-deoxycorticosterone. Thus, at least two distinct cytochrome P-450(11) beta species exist in the adrenal cortex and participate in steroidogenesis.
Ogishima
T
T
Department of Biochemistry, School of Medicine, Keio University, Tokyo.
Mitani
F
F
Ishimura
Y
Y
D000302:Adrenal Cortex / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D012967:Sodium Dodecyl Sulfate; D013252:Steroid 11-beta-Hydroxylase / Q000032:analysis / Q000302:isolation & purification*; D013250:Steroid Hydroxylases / Q000302:isolation & purification*
D012967:Sodium Dodecyl Sulfate; D013250:Steroid Hydroxylases; D013252:Steroid 11-beta-Hydroxylase