Abstract:
:Cytochrome b(5) (cyt-b(5)) is essential for the regulation of steroidogenesis and as such has been implicated in a number of clinical conditions. It is well documented that this small hemoprotein augments the 17,20-lyase activity of cytochrome P450 17α-hydroxylase/17,20-lyase (CYP17A1). Studies have revealed that this augmentation is accomplished by cyt-b(5) enhancing the interaction between cytochrome P450 reductase (POR) and CYP17A1. In this paper we present evidence that cyt-b(5) induces a conformational change in CYP17A1, in addition to facilitating the interaction between CYP17A1 and POR. We also review the recently published finding that cyt-b(5) allosterically augments the activity of 3β-hydroxysteroid dehydrogenase/Δ(5)-Δ(4) isomerase (3βHSD), a non cytochrome P450 enzyme, by increasing the enzymes affinity for its cofactor, NAD(+). The physiological importance of this finding, in terms of understanding adrenal androstenedione production, is examined. Finally, evidence that cyt-b(5) is able to form homomeric complexes in living cells is presented and discussed.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
Storbeck KH,Swart AC,Goosen P,Swart Pdoi
10.1016/j.mce.2012.11.020subject
Has Abstractpub_date
2013-05-22 00:00:00pages
87-99issue
1-2eissn
0303-7207issn
1872-8057pii
S0303-7207(12)00512-6journal_volume
371pub_type
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