High impact information on Andien-beta

• The formation of 5,16-androstadien-3 beta-ol from pregnenolone (andien-beta synthase activity) is catalyzed by cytochrome P450c17, which also catalyzes C-17-hydroxy/lyase activity in the biosynthesis of androgens [1].
• However, when cytochrome b5 isolated from porcine testis was added, andien-beta synthase activity was detected in all three preparations of cytochrome P450c17, with the highest activity found in the porcine preparations [2].
• Andien-beta synthase activity in testis microsomes was inhibited by high pH and concentration of salt, while C17-hydroxylase/lyase activity was stimulated under these conditions [2].
• Cytochrome P-450SCCII catalyses the formation of the first C19 androgen intermediates, while the enzyme system that catalyzes the formation of the first androst-16-ene intermediates, so called andien-beta synthase, has not previously been well characterized [3].

Anatomical context of Andien-beta

• Andien-beta synthase is very active in porcine Leydig cells, but it is almost undetectable in porcine and bovine adrenal, although the adrenal gland also expresses P450c17 [1].

Associations of Andien-beta with other chemical compounds

• Formation of androstadienone or androstadienol, a delta 16-C19-steroid, from progesterone or pregnenolone is catalyzed by the so-called delta 16-C19-steroid synthesizing enzyme in the pig testicular microsomes [4].

Gene context of Andien-beta

• It appears that the andien-beta synthase activity is catalysed by cytochrome P450c17, which is not unique to the porcine testis and is dependent upon adequate levels of cytochrome b5 [2].

References