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| Name = 3-ketosteroid 9alpha-monooxygenase
| EC_number = 1.14.13.142
| CAS_number =
| IUBMB_EC_number = 1/14/13/142
| GO_code =
| image =
| width =
| caption =
}}3-ketosteroid 9alpha-monooxygenase ({{EC number|1.14.13.142}}, KshAB, 3-ketosteroid 9alpha-hydroxylase) is an enzyme with systematic name androsta-1,4-diene-3,17-dione,NADH:oxygen oxidoreductase (9alpha-hydroxylating).[1][2][3] This enzyme catalyses the following chemical reaction
androsta-1,4-diene-3,17-dione + NADH + H+ + O29alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
3-Ketosteroid 9alpha-monooxygenase is involved in the cholesterol degradation in several bacterial pathogens.
References
1. ^{{cite journal | vauthors = Petrusma M, Dijkhuizen L, van der Geize R | title = Rhodococcus rhodochrous DSM 43269 3-ketosteroid 9alpha-hydroxylase, a two-component iron-sulfur-containing monooxygenase with subtle steroid substrate specificity | journal = Applied and Environmental Microbiology | volume = 75 | issue = 16 | pages = 5300–7 | date = August 2009 | pmid = 19561185 | pmc = 2725467 | doi = 10.1128/AEM.00066-09 }}
2. ^{{cite journal | vauthors = Capyk JK, D'Angelo I, Strynadka NC, Eltis LD | title = Characterization of 3-ketosteroid 9{alpha}-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis | journal = The Journal of Biological Chemistry | volume = 284 | issue = 15 | pages = 9937–46 | date = April 2009 | pmid = 19234303 | pmc = 2665117 | doi = 10.1074/jbc.M900719200 }}
3. ^{{cite journal | vauthors = Capyk JK, Casabon I, Gruninger R, Strynadka NC, Eltis LD | title = Activity of 3-ketosteroid 9α-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosis | journal = The Journal of Biological Chemistry | volume = 286 | issue = 47 | pages = 40717–24 | date = November 2011 | pmid = 21987574 | pmc = 3220451 | doi = 10.1074/jbc.M111.289975 }}
2. ^{{cite journal | vauthors = Capyk JK, D'Angelo I, Strynadka NC, Eltis LD | title = Characterization of 3-ketosteroid 9{alpha}-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis | journal = The Journal of Biological Chemistry | volume = 284 | issue = 15 | pages = 9937–46 | date = April 2009 | pmid = 19234303 | pmc = 2665117 | doi = 10.1074/jbc.M900719200 }}
3. ^{{cite journal | vauthors = Capyk JK, Casabon I, Gruninger R, Strynadka NC, Eltis LD | title = Activity of 3-ketosteroid 9α-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosis | journal = The Journal of Biological Chemistry | volume = 286 | issue = 47 | pages = 40717–24 | date = November 2011 | pmid = 21987574 | pmc = 3220451 | doi = 10.1074/jbc.M111.289975 }}
External links
- {{MeshName|3-ketosteroid+9alpha-monooxygenase}}
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