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Ketosteroid monooksigenaza
Identifikatori
EC broj	1.14.13.54
CAS broj	9044-53-5
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Ketosteroid monooksigenaza (EC 1.14.13.54, steroid-ketonska monooksigenaza, progesteron, NADPH₂:kiseonik oksidoreduktaza (20-hidroksilacija, formiranje estra), 17alfa-hidroksiprogesteron, NADPH₂:kiseonik oksidoreduktaza (20-hidroksilacija, odvajanje bočnog lanca), androstendion, NADPH₂:kiseonik oksidoreduktaza (17-hidroksilacija, laktonizacija)) je enzim sa sistematskim imenom ketosteroid,NADPH:kiseonik oksidoreduktaza (20-hidroksilacija, formiranje estra/20-hidroksilacija, odvajanje bočnog lanca/17-hidroksilacija, laktonizacija).^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

ketosteroid + NADPH + H⁺ + O₂

\rightleftharpoons

steroid estar/lakton + NADP⁺ + H₂O (opšta reakcija)

(1) progesteron + NADPH + H⁺ + O₂

\rightleftharpoons

testosteron acetat + NADP⁺ + H₂O

(2) androstendion + NADPH + H⁺ + O₂

\rightleftharpoons

testololakton + NADP⁺ + H₂O

(3) 17alfa-hidroksiprogesteron + NADPH + H⁺ + O₂

\rightleftharpoons

androstendion + acetat + NADP⁺ +H₂O

Ovaj enzim sadrži jednu FAD grupu. On katalizuje tri tipa monooksigenaznih reakcija.

Reference

↑ Katagiri, M. and Itagaki, E. (1991). „A steroid ketone monooxygenase from Cylindrocarpon radicicola”. u: Müller, F.. Chemistry and Biochemistry of Flavoenzymes. Florida: CRC Press. str. 102-108.
↑ Itagaki, E. (1986). „Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization”. J. Biochem. (Tokyo) 99: 815-824. PMID 3486863.
↑ Itagaki, E. (1986). „Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC11011. Oxygenative lactonization of androstenedione to testololactone”. J. Biochem. (Tokyo) 99: 825-832. PMID 3486864.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Katagiri, M. and Itagaki, E. (1991). „A steroid ketone monooxygenase from Cylindrocarpon radicicola”. u: Müller, F.. Chemistry and Biochemistry of Flavoenzymes. Florida: CRC Press. str. 102-108.

Vanjske veze

MeSH Ketosteroid+monooxygenase

[1] Katagiri, M. and Itagaki, E. (1991). „A steroid ketone monooxygenase from Cylindrocarpon radicicola”. u: Müller, F.. Chemistry and Biochemistry of Flavoenzymes. Florida: CRC Press. str. 102-108.

[2] Itagaki, E. (1986). „Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization”. J. Biochem. (Tokyo) 99: 815-824. PMID 3486863.

[3] Itagaki, E. (1986). „Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC11011. Oxygenative lactonization of androstenedione to testololactone”. J. Biochem. (Tokyo) 99: 825-832. PMID 3486864.

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