Ketosteroid monooxygenase
In today's world, Ketosteroid monooxygenase is a topic of great relevance and interest to a wide spectrum of people. Whether due to its impact on society, its importance in history or its relevance in today's world, Ketosteroid monooxygenase has become a topic that arouses passions, conflicting opinions and heated debates. From academia to the workplace, Ketosteroid monooxygenase has managed to capture the attention and interest of experts and neophytes alike. In this article, we will explore different aspects of Ketosteroid monooxygenase, analyzing its impact on various spheres of life and its relevance to understanding the world around us.
| Ketosteroid monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.54 | ||||||||
| CAS no. | 9044-53-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Ketosteroid monooxygenase (EC 1.14.13.54, steroid-ketone monooxygenase, progesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, ester-producing), 17alpha-hydroxyprogesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, side-chain cleaving), androstenedione, NADPH2:oxygen oxidoreductase (17-hydroxylating, lactonizing)) is an enzyme with systematic name ketosteroid, NADPH:oxygen oxidoreductase (20-hydroxylating, ester-producing/20-hydroxylating, side-chain cleaving/17-hydroxylating, lactonizing).[1][2][3] This enzyme catalyses the following chemical reaction
- ketosteroid + NADPH + H+ + O2 steroid ester/lactone + NADP+ + H2O (general reaction)
- (1) progesterone + NADPH + H+ + O2 testosterone acetate + NADP+ + H2O
- (2) androstenedione + NADPH + H+ + O2 testololactone + NADP+ + H2O
- (3) 17alpha-hydroxyprogesterone + NADPH + H+ + O2 androstenedione + acetate + NADP+ + H2O
Ketosteroid monooxygenase is a single FAD-containing enzyme that catalyses three types of monooxygenase reaction.
References
- ^ Katagiri M, Itagaki E (1991). "A steroid ketone monooxygenase from Cylindrocarpon radicicola". In Muller F (ed.). Chemistry and Biochemistry of Flavoenzymes. Florida: CRC Press. pp. 102–108.
- ^ Itagaki E (March 1986). "Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization". Journal of Biochemistry. 99 (3): 815–24. PMID 3486863.
- ^ Itagaki E (March 1986). "Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Oxygenative lactonization of androstenedione to testololactone". Journal of Biochemistry. 99 (3): 825–32. PMID 3486864.
External links
- Ketosteroid+monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
