KEGG   ENZYME: 1.14.15.28
Entry
EC 1.14.15.28               Enzyme                                 

Name
cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming];
CYP142
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
cholest-4-en-3-one,reduced [2Fe-2S] ferredoxin:oxygen oxidoreductase [(25R)-3-oxocholest-4-en-26-oate forming]
Reaction(IUBMB)
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O (overall reaction) [RN:R11361];
(1a) cholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-26-hydroxycholest-4-en-3-one + 2 oxidized [2Fe-2S] ferredoxin + H2O [RN:R11358];
(1b) (25R)-26-hydroxycholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-26-oxocholest-4-en-3-one + 2 oxidized [2Fe-2S] ferredoxin + 2 H2O [RN:R11359];
(1c) (25R)-26-oxocholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-3-oxocholest-4-en-26-oate + 2 oxidized [2Fe-2S] ferredoxin + H2O [RN:R11360]
Reaction(KEGG)
Substrate
cholest-4-en-3-one [CPD:C00599];
reduced [2Fe-2S] ferredoxin [CPD:C22150];
O2 [CPD:C00007];
(25R)-26-hydroxycholest-4-en-3-one [CPD:C21303];
(25R)-26-oxocholest-4-en-3-one [CPD:C21305]
Product
(25R)-3-oxocholest-4-en-26-oate [CPD:C20839];
oxidized [2Fe-2S] ferredoxin [CPD:C22151];
H2O [CPD:C00001];
(25R)-26-hydroxycholest-4-en-3-one [CPD:C21303];
(25R)-26-oxocholest-4-en-3-one [CPD:C21305]
Comment
This cytochrome P-450 (heme-thiolate) enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol. It catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25R) conformation. The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.15.29, cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]. The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet.
History
EC 1.14.15.28 created 2016 as EC 1.14.13.221, transferred 2018 to EC 1.14.15.28
Pathway
ec00984  Steroid degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K16046  cholest-4-en-3-one 26-monooxygenase
Genes
MTU: Rv3518c(cyp142)
MTV: RVBD_3518c
MTC: MT3619
MRA: MRA_3557(cyp142)
MTF: TBFG_13551
MTB: TBMG_03557
MTK: TBSG_03584
MTZ: TBXG_003533
MTG: MRGA327_21740
MTI: MRGA423_22200
MTUR: CFBS_3734(cyp142)
MTO: MTCTRI2_3582(cyp142)
MTD: UDA_3518c(cyp142)
MTN: ERDMAN_3857(cyp142)
MTUC: J113_24605
MTUE: J114_18810
MTUH: I917_24680
MTUL: TBHG_03458
MTUT: HKBT1_3719(cyp142)
MTUU: HKBT2_3728(cyp142)
MTQ: HKBS1_3731(cyp142)
MBO: BQ2027_MB3547C(cyp142b) BQ2027_MB3548C(cyp142a)
MBB: BCG_3581c(cyp142b) BCG_3582c(cyp142a)
MBT: JTY_3582(cyp142b) JTY_3583(cyp142a)
MBM: BCGMEX_3579c(cyp142b) BCGMEX_3580c(cyp142a)
MBX: BCGT_3381
MCE: MCAN_35291(cyp142)
MCQ: BN44_110006(cyp)
MCV: BN43_90011(cyp)
MCX: BN42_90009(cyp)
MCZ: BN45_100009(cyp)
MPA: MAP_0547
MAO: MAP4_3320
MAVI: RC58_16465
MAVU: RE97_16500
MAV: MAV_0641
MLP: MLM_0784
MUL: MUL_4077(cyp142A3)
MMC: Mmcs_4631
MKM: Mkms_4719
MJL: Mjls_5013
MMI: MMAR_5003(cyp142A3)
MMAE: MMARE11_48130(cyp142A3)
MLI: MULP_05251(cyp142A3)
MHAD: B586_04705
MSHG: MSG_04505(cyp142)
MFJ: MFLOJ_41190(cyp142)
MXE: MYXE_06290(cyp142)
MNV: MNVI_12010(cyp142)
MSG: MSMEI_5758(cyp142)
MVA: Mvan_5217
MGI: Mflv_1541
MVQ: MYVA_5103
MHAS: MHAS_03703
MMAG: MMAD_47780
MMOR: MMOR_12480(cyp142_2)
MJD: JDM601_3652(cyp142A3)
MTER: 4434518_03626(cyp142A3)
MMIN: MMIN_11820
MHIB: MHIB_30500
MKR: MKOR_35990(cyp142)
RER: RER_07670
REY: O5Y_03730
ROP: ROP_45330
REQ: REQ_06880
TCU: Tcur_2583
SRO: Sros_7155
 » show all
Reference
1  [PMID:20889498]
  Authors
Driscoll MD, McLean KJ, Levy C, Mast N, Pikuleva IA, Lafite P, Rigby SE, Leys D, Munro AW
  Title
Structural and biochemical characterization of Mycobacterium tuberculosis CYP142: evidence for multiple cholesterol 27-hydroxylase activities in a human pathogen.
  Journal
J Biol Chem 285:38270-82 (2010)
DOI:10.1074/jbc.M110.164293
  Sequence
[mtu:Rv3518c]
Reference
2  [PMID:20843794]
  Authors
Johnston JB, Ouellet H, Ortiz de Montellano PR
  Title
Functional redundancy of steroid C26-monooxygenase activity in Mycobacterium tuberculosis revealed by biochemical and genetic analyses.
  Journal
J Biol Chem 285:36352-60 (2010)
DOI:10.1074/jbc.M110.161117
  Sequence
[mtu:Rv3518c]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.15.28
IUBMB Enzyme Nomenclature: 1.14.15.28
ExPASy - ENZYME nomenclature database: 1.14.15.28
BRENDA, the Enzyme Database: 1.14.15.28

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