KEGG   ORTHOLOGY: K16046
Entry
K16046                      KO                                     
Symbol
CYP142
Name
cholest-4-en-3-one 26-monooxygenase [EC:1.14.15.28]
Pathway
map00984  Steroid degradation
map01120  Microbial metabolism in diverse environments
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09111 Xenobiotics biodegradation and metabolism
   00984 Steroid degradation
    K16046  CYP142; cholest-4-en-3-one 26-monooxygenase
 09180 Brite Hierarchies
  09181 Protein families: metabolism
   00199 Cytochrome P450
    K16046  CYP142; cholest-4-en-3-one 26-monooxygenase
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.14  Acting on paired donors, with incorporation or reduction of molecular oxygen
   1.14.15  With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
    1.14.15.28  cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]
     K16046  CYP142; cholest-4-en-3-one 26-monooxygenase
Cytochrome P450 [BR:ko00199]
 Cytochrome P450, bacteria type
  CYP142 family
   K16046  CYP142; cholest-4-en-3-one 26-monooxygenase
Other DBs
RN: R11358 R11359 R11360 R11361
COG: COG2124
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
MMAN: MMAN_43780(cyp142) MMAN_48470
MUL: MUL_4077(cyp142A3)
MMI: MMAR_5003(cyp142A3)
MMAE: MMARE11_48130(cyp142A3)
MLI: MULP_05251(cyp142A3)
MPSE: MPSD_52010(cyp142)
MSHO: MSHO_04690(cyp142)
MMC: Mmcs_4631
MKM: Mkms_4719
MJL: Mjls_5013
MHAD: B586_04705
MSHG: MSG_04505(cyp142)
MFJ: MFLOJ_41190(cyp142)
MSTO: MSTO_45170(cyp142)
MSIM: MSIM_29590(cyp142) MSIM_48400
MSAK: MSAS_28600
MXE: MYXE_06290(cyp142)
MNV: MNVI_12010(cyp142)
MCOO: MCOO_26630(cyp142)
MSEO: MSEO_33990(cyp142)
MHEK: JMUB5695_00528(cyp142)
MGAU: MGALJ_37780(cyp142)
MLJ: MLAC_00250(cyp142)
MBRD: MBRA_14020(cyp142) MBRA_20550
MSHJ: MSHI_39220(cyp142)
MKR: MKOR_35990(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)
MALV: MALV_43030
MARZ: MARA_48660
MGAD: MGAD_36860(cyp142)
MHEV: MHEL_08790(cyp142) MHEL_28410
MAUB: MAUB_26100
MPOF: MPOR_53180
MPHU: MPHO_44250
MBOK: MBOE_03720
MCEE: MCEL_38510(cyp142)
MJD: JDM601_3652(cyp142A3)
MTER: 4434518_03626(cyp142A3)
MMIN: MMIN_11820
MHIB: MHIB_30500
RER: RER_07670
REY: O5Y_03730
ROP: ROP_45330
REQ: REQ_06880
TCU: Tcur_2583
SRO: Sros_7155
 » show all
Reference
PMID:20843794 (CYP142A1)
  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]

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)
MMIMMAR_5003(cyp142A3)
MMAEMMARE11_48130(cyp142A3)
MLIMULP_05251(cyp142A3)
MPSEMPSD_52010(cyp142)
MSHOMSHO_04690(cyp142)
MMCMmcs_4631
MKMMkms_4719
MJLMjls_5013
MMMW7S_00635 W7S_02700
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)
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)
MMONEWR22_25045
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
RPSKJWS13_19265
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

KEGG   REACTION: R11361
Entry
R11361                      Reaction                               
Name
cholest-4-en-3-one,reduced-2Fe-2S]-ferredoxin:oxygen oxidoreductase [(25R)-3-oxocholest-4-en-26-oate forming]
Definition
Cholest-4-en-3-one + 6 Reduced [2Fe-2S] ferredoxin + 3 Oxygen <=> (25R)-3-Oxocholest-4-en-26-oate + 6 Oxidized [2Fe-2S] ferredoxin + 4 H2O
Equation
C00599 + 6 C22150 + 3 C00007 <=> C20839 + 6 C22151 + 4 C00001
Comment
three-step reaction (see R11358+R11359+R11360)
Reaction class
RC03368  C00599_C20839
Enzyme
Pathway
rn00984  Steroid degradation
rn01120  Microbial metabolism in diverse environments
Orthology
K16046  cholest-4-en-3-one 26-monooxygenase [EC:1.14.15.28]
Other DBs
RHEA: 49999

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