Ketosteroid monooxygenase

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
Search PMC articles PubMed articles NCBI proteins

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${\displaystyle \rightleftharpoons }$ steroid ester/lactone + NADP⁺ + H₂O (general reaction)

(1) progesterone + NADPH + H⁺ + O₂${\displaystyle \rightleftharpoons }$ testosterone acetate + NADP⁺ + H₂O

(2) androstenedione + NADPH + H⁺ + O₂${\displaystyle \rightleftharpoons }$ testololactone + NADP⁺ + H₂O

(3) 17alpha-hydroxyprogesterone + NADPH + H⁺ + O₂${\displaystyle \rightleftharpoons }$ androstenedione + acetate + NADP⁺ + H₂O

Ketosteroid monooxygenase is a single FAD-containing enzyme that catalyses three types of monooxygenase reaction.

References

1. 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.
2. Itagaki E (March 1986). "Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization". Journal of Biochemistry. 99 (3): 815–24. doi: 10.1093/oxfordjournals.jbchem.a135541 . PMID   3486863.
3. 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. doi: 10.1093/oxfordjournals.jbchem.a135542 . PMID   3486864.

External links

• Ketosteroid+monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)