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
MTURv3518c(cyp142)
MTVRVBD_3518c
MTCMT3619
MRAMRA_3557(cyp142)
MTFTBFG_13551
MTBTBMG_03557
MTKTBSG_03584
MTZTBXG_003533
MTGMRGA327_21740
MTIMRGA423_22200
MTECCDC5079_3259
MTURCFBS_3734(cyp142)
MTLCCDC5180_3211
MTOMTCTRI2_3582(cyp142)
MTDUDA_3518c(cyp142)
MTNERDMAN_3857(cyp142)
MTJJ112_18940
MTUBMT7199_3578
MTUCJ113_24605
MTUEJ114_18810
MTXM943_18090
MTUHI917_24680
MTULTBHG_03458
MTUTHKBT1_3719(cyp142)
MTUUHKBT2_3728(cyp142)
MTQHKBS1_3731(cyp142)
MBOBQ2027_MB3547C(cyp142b) BQ2027_MB3548C(cyp142a)
MBBBCG_3581c(cyp142b) BCG_3582c(cyp142a)
MBTJTY_3582(cyp142b) JTY_3583(cyp142a)
MBMBCGMEX_3579c(cyp142b) BCGMEX_3580c(cyp142a)
MBKK60_036520 K60_036530
MBXBCGT_3381
MMICRN08_3892 RN08_3893
MCEMCAN_35291(cyp142)
MCQBN44_110006(cyp)
MCVBN43_90011(cyp)
MCXBN42_90009(cyp)
MCZBN45_100009(cyp)
MPAMAP_0547
MAOMAP4_3320
MAVIRC58_16465
MAVURE97_16500
MAVMAV_0641
MITOCO_01300 OCO_05500
MIAOCU_01340 OCU_05550
MIDMIP_00395 MIP_01006
MYOOEM_01390 OEM_05580
MCHIAN480_00700 AN480_02755
MIROCQ_01290 OCQ_05660
MMALCKJ54_00570 CKJ54_02680
MLPMLM_0784
MMANMMAN_43780(cyp142) MMAN_48470
MSAMycsm_05751
MULMUL_4077(cyp142A3)
MMCMmcs_4631
MKMMkms_4719
MJLMjls_5013
MMIMMAR_5003(cyp142A3)
MMAEMMARE11_48130(cyp142A3)
MMMW7S_00635 W7S_02700
MLIMULP_05251(cyp142A3)
MKNMKAN_11750
MYVG155_04820
MYEAB431_06755 AB431_26265
MGOAFA91_11165
MHADB586_04705
MDXBTO20_31100
MSHGMSG_04505(cyp142)
MFJMFLOJ_41190(cyp142)
MSTOMSTO_45170(cyp142)
MSIMMSIM_29590(cyp142) MSIM_48400
MSAKMSAS_28600
MKUI2456_06630 I2456_25405
MGROFZ046_02520
MXEMYXE_06290(cyp142)
MNVMNVI_12010(cyp142)
MPAGC0J29_27450
MNMMNVM_24280
MGORH0P51_00720 H0P51_25500
MCOOMCOO_26630(cyp142)
MBAIMB901379_04397
MSEOMSEO_33990(cyp142)
MPSEMPSD_52010(cyp142)
MSHOMSHO_04690(cyp142)
MHEKJMUB5695_00528(cyp142)
MGAUMGALJ_37780(cyp142)
MLJMLAC_00250(cyp142)
MBRDMBRA_14020(cyp142) MBRA_20550
MSHJMSHI_39220(cyp142)
MKRMKOR_35990(cyp142)
MDFK0O62_25325
MMAMK3U93_22385
MHOLK3U96_03410
MHERK3U94_20645
MSENK3U95_25000
MPAEK0O64_06385 K0O64_25755
MSPGF6B93_20205
MOTLTS72_00080
MVMMJO54_20580
MRFMJO55_23815
MPAAMKK62_02690
MCROMI149_07090 MI149_26065
MSMMSMEG_5918
MSGMSMEI_5758(cyp142)
MSBLJ00_29265
MSNLI99_29270
MSHLI98_29275
MVAMvan_5217
MGIMflv_1541
MSPMspyr1_09250
MCBMycch_4578
MNED174_24160
MYNMyAD_23700
MFTXA26_09260
MPHLMPHLCCUG_00591
MVQMYVA_5103
MLLB1R94_06765 B1R94_24805
MRHMycrhN_2317
MTHN4412656_04035
MHASMHAS_03703
MDUMDUV_49910
MCHTMCHIJ_20130
MAUUNCTC10437_04981
MMAGMMAD_47780
MMORMMOR_12480(cyp142_2)
MFXMFAL_33760
MAICMAIC_05950 MAIC_42210
MIJMINS_43060
MALVMALV_43030
MTYMTOK_23080
MPSCMPSYJ_16480
MARZMARA_48660
MGADMGAD_36860(cyp142)
MHEVMHEL_08790(cyp142) MHEL_28410
MSARMSAR_10370 MSAR_27650
MANYMANY_25750 MANY_32410
MAUBMAUB_26100
MPOFMPOR_53180
MPHUMPHO_44250
MMUCC1S78_025160
MMATMMAGJ_35060
MBOKMBOE_03720
MFGK6L26_05830
MSEIMSEDJ_01750
MFLVNCTC10271_00535
MCEEMCEL_38510(cyp142)
MJDJDM601_3652(cyp142A3)
MTER4434518_03626(cyp142A3)
MMINMMIN_11820
MHIBMHIB_30500
MPAKMIU77_02280
RHARHA1_ro04588
RERRER_07670
REYO5Y_03730
REBXU06_03970
RQIC1M55_04210
ROPROP_45330
ROAPd630_LPD01065
RHWBFN03_15100
RHODAOT96_14605
RKOJWS14_25270
RGOKYT97_23305
ROZCBI38_04260
REQREQ_06880
YIALO772_20455
TCUTcur_2583
ACTWF7P10_01990
AGRAAGRA3207_002188
SROSros_7155
NOABKM31_57860
NGNLCN96_42985
FRIFraEuI1c_2049 FraEuI1c_2543
PBROHOP40_00280
ABAIIMCC26256_11539
AYMYM304_15670
AQZKSP35_16625
IAMHC251_00840 HC251_06765
 » 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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