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Steroid C26-monooxygenase (EC 1.14.15.28) (Cholest-4-en-3-one C26-monooxygenase) (Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]) (Cholesterol C26-monooxygenase) (Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming]) (Cytochrome P450 142) (Steroid C27-monooxygenase)

 CP142_MYCTU             Reviewed;         398 AA.
P9WPL5; D0EW73; F2GEM8; O53563;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
11-DEC-2019, entry version 38.
RecName: Full=Steroid C26-monooxygenase {ECO:0000303|PubMed:20843794};
EC=1.14.15.28 {ECO:0000269|PubMed:20843794, ECO:0000269|PubMed:20889498, ECO:0000305|PubMed:25210044};
AltName: Full=Cholest-4-en-3-one C26-monooxygenase {ECO:0000303|PubMed:20843794};
AltName: Full=Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] {ECO:0000303|PubMed:20843794};
AltName: Full=Cholesterol C26-monooxygenase {ECO:0000303|PubMed:20843794};
AltName: Full=Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming] {ECO:0000303|PubMed:20843794};
AltName: Full=Cytochrome P450 142 {ECO:0000303|PubMed:20889498};
AltName: Full=Steroid C27-monooxygenase {ECO:0000303|PubMed:20889498};
Name=cyp142; Synonyms=cyp142A1 {ECO:0000303|PubMed:20843794};
OrderedLocusNames=Rv3518c; ORFNames=MTV023.25c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Vasilevskaya A.V., Alyapkina Y.S., Usanov S.A.;
"Polymorphism of cytochrome P450 of drug resistant form of Mycobacterium
tuberculosis.";
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the complete
genome sequence.";
Nature 393:537-544(1998).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
SUBSTRATE SPECIFICITY, INDUCTION, AND PATHWAY.
PubMed=20843794; DOI=10.1074/jbc.m110.161117;
Johnston J.B., Ouellet H., Ortiz de Montellano P.R.;
"Functional redundancy of steroid C26-monooxygenase activity in
Mycobacterium tuberculosis revealed by biochemical and genetic analyses.";
J. Biol. Chem. 285:36352-36360(2010).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.m111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=25210044; DOI=10.1074/jbc.m114.602771;
Frank D.J., Madrona Y., Ortiz de Montellano P.R.;
"Cholesterol ester oxidation by mycobacterial cytochrome P450.";
J. Biol. Chem. 289:30417-30425(2014).
[6]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY
REGULATION, AND SUBSTRATE SPECIFICITY.
PubMed=20889498; DOI=10.1074/jbc.m110.164293;
Driscoll M.D., McLean K.J., Levy C., Mast N., Pikuleva I.A., Lafite P.,
Rigby S.E., Leys D., Munro A.W.;
"Structural and biochemical characterization of Mycobacterium tuberculosis
CYP142: evidence for multiple cholesterol 27-hydroxylase activities in a
human pathogen.";
J. Biol. Chem. 285:38270-38282(2010).
-!- FUNCTION: Involved in the utilization of cholesterol as the sole carbon
and energy source by degrading the side chain during infection
(PubMed:20843794). Primarily catalyzes the sequential oxidation of the
terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-
en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to
finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate
(PubMed:20843794, PubMed:20889498). In vitro, Cyp142 catalyzes with
equal preference the oxidation of both (25R)- and (25S)-26-
hydroxycholest-4-en-3-one diastereomers to the corresponding carboxylic
acid which is a prerequisite for entry into the beta-oxidation pathway
(PubMed:20843794). Also able to sequentially oxidize cholesterol
itself, not only cholest-4-en-3-one (PubMed:20843794).
{ECO:0000269|PubMed:20843794, ECO:0000269|PubMed:20889498,
ECO:0000269|PubMed:25210044}.
-!- CATALYTIC ACTIVITY:
Reaction=cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-
[ferredoxin] = (25R)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized
[2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:49996, Rhea:RHEA-COMP:10000,
Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, ChEBI:CHEBI:33737,
ChEBI:CHEBI:33738, ChEBI:CHEBI:71570; EC=1.14.15.28;
Evidence={ECO:0000269|PubMed:20843794, ECO:0000269|PubMed:20889498,
ECO:0000305|PubMed:25210044};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:20843794, ECO:0000269|PubMed:20889498,
ECO:0000269|PubMed:25210044};
-!- ACTIVITY REGULATION: Inhibited by econazole, clotrimazole and
miconazole. {ECO:0000269|PubMed:20889498}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.2 uM for cholest-4-en-3-one {ECO:0000269|PubMed:20889498};
KM=7.7 uM for cholesterol {ECO:0000269|PubMed:20843794};
KM=9.2 uM for cholesteryl sulfate {ECO:0000269|PubMed:25210044};
KM=11.8 uM for cholest-4-en-3-one {ECO:0000269|PubMed:20843794};
Note=Kcat is 84 min(-1) for cholest-4-en-3-one as substrate
(PubMed:20843794). Kcat is 16.7 min(-1) for cholesterol as substrate
(PubMed:20843794). Kcat is 0.0062 min(-1) for cholest-4-en-3-one as
substrate (PubMed:20889498). {ECO:0000269|PubMed:20843794,
ECO:0000269|PubMed:20889498};
-!- PATHWAY: Steroid metabolism; cholesterol degradation.
{ECO:0000305|PubMed:20843794}.
-!- INDUCTION: By cholesterol. {ECO:0000305|PubMed:20843794}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; GQ900521; ACX47920.1; -; Genomic_DNA.
EMBL; AL123456; CCP46340.1; -; Genomic_DNA.
PIR; H70807; H70807.
RefSeq; NP_218035.1; NC_000962.3.
RefSeq; WP_003900082.1; NZ_NVQJ01000014.1.
PDB; 2XKR; X-ray; 1.60 A; A=1-398.
PDBsum; 2XKR; -.
SMR; P9WPL5; -.
STRING; 83332.Rv3518c; -.
SwissLipids; SLP:000001011; -.
PaxDb; P9WPL5; -.
EnsemblBacteria; CCP46340; CCP46340; Rv3518c.
GeneID; 888282; -.
KEGG; mtu:Rv3518c; -.
KEGG; mtv:RVBD_3518c; -.
TubercuList; Rv3518c; -.
eggNOG; ENOG4111GWC; LUCA.
KO; K16046; -.
OMA; AGIHFCI; -.
PhylomeDB; P9WPL5; -.
BioCyc; MetaCyc:G185E-7795-MONOMER; -.
BioCyc; MTBH37RV:G185E-7795-MONOMER; -.
UniPathway; UPA01058; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; HDA:MTBBASE.
GO; GO:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; IDA:MTBBASE.
GO; GO:0031073; F:cholesterol 26-hydroxylase activity; IDA:MTBBASE.
GO; GO:0020037; F:heme binding; IDA:MTBBASE.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0006707; P:cholesterol catabolic process; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR002397; Cyt_P450_B.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00359; BP450.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Cholesterol metabolism; Heme; Iron; Lipid degradation;
Lipid metabolism; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
Reference proteome; Steroid metabolism; Sterol metabolism; Virulence.
CHAIN 1..398
/note="Steroid C26-monooxygenase"
/id="PRO_0000052304"
METAL 340
/note="Iron (heme axial ligand)"
/evidence="ECO:0000244|PDB:2XKR,
ECO:0000269|PubMed:20889498"
HELIX 12..15
/evidence="ECO:0000244|PDB:2XKR"
HELIX 20..30
/evidence="ECO:0000244|PDB:2XKR"
STRAND 32..35
/evidence="ECO:0000244|PDB:2XKR"
STRAND 41..43
/evidence="ECO:0000244|PDB:2XKR"
HELIX 46..53
/evidence="ECO:0000244|PDB:2XKR"
TURN 56..58
/evidence="ECO:0000244|PDB:2XKR"
STRAND 59..61
/evidence="ECO:0000244|PDB:2XKR"
HELIX 75..77
/evidence="ECO:0000244|PDB:2XKR"
HELIX 82..90
/evidence="ECO:0000244|PDB:2XKR"
HELIX 91..93
/evidence="ECO:0000244|PDB:2XKR"
HELIX 96..100
/evidence="ECO:0000244|PDB:2XKR"
HELIX 103..115
/evidence="ECO:0000244|PDB:2XKR"
TURN 116..120
/evidence="ECO:0000244|PDB:2XKR"
STRAND 121..124
/evidence="ECO:0000244|PDB:2XKR"
HELIX 125..128
/evidence="ECO:0000244|PDB:2XKR"
TURN 129..131
/evidence="ECO:0000244|PDB:2XKR"
HELIX 132..142
/evidence="ECO:0000244|PDB:2XKR"
HELIX 146..148
/evidence="ECO:0000244|PDB:2XKR"
HELIX 149..163
/evidence="ECO:0000244|PDB:2XKR"
HELIX 169..195
/evidence="ECO:0000244|PDB:2XKR"
HELIX 201..207
/evidence="ECO:0000244|PDB:2XKR"
HELIX 217..231
/evidence="ECO:0000244|PDB:2XKR"
HELIX 233..248
/evidence="ECO:0000244|PDB:2XKR"
HELIX 250..258
/evidence="ECO:0000244|PDB:2XKR"
HELIX 260..262
/evidence="ECO:0000244|PDB:2XKR"
HELIX 263..274
/evidence="ECO:0000244|PDB:2XKR"
STRAND 279..286
/evidence="ECO:0000244|PDB:2XKR"
STRAND 288..290
/evidence="ECO:0000244|PDB:2XKR"
STRAND 293..295
/evidence="ECO:0000244|PDB:2XKR"
STRAND 300..304
/evidence="ECO:0000244|PDB:2XKR"
HELIX 305..309
/evidence="ECO:0000244|PDB:2XKR"
TURN 312..314
/evidence="ECO:0000244|PDB:2XKR"
STRAND 315..317
/evidence="ECO:0000244|PDB:2XKR"
HELIX 343..360
/evidence="ECO:0000244|PDB:2XKR"
STRAND 365..367
/evidence="ECO:0000244|PDB:2XKR"
STRAND 379..381
/evidence="ECO:0000244|PDB:2XKR"
STRAND 388..390
/evidence="ECO:0000244|PDB:2XKR"
SEQUENCE 398 AA; 44399 MW; BCFF3C23ECB5767F CRC64;
MTEAPDVDLA DGNFYASREA RAAYRWMRAN QPVFRDRNGL AAASTYQAVI DAERQPELFS
NAGGIRPDQP ALPMMIDMDD PAHLLRRKLV NAGFTRKRVK DKEASIAALC DTLIDAVCER
GECDFVRDLA APLPMAVIGD MLGVRPEQRD MFLRWSDDLV TFLSSHVSQE DFQITMDAFA
AYNDFTRATI AARRADPTDD LVSVLVSSEV DGERLSDDEL VMETLLILIG GDETTRHTLS
GGTEQLLRNR DQWDLLQRDP SLLPGAIEEM LRWTAPVKNM CRVLTADTEF HGTALCAGEK
MMLLFESANF DEAVFCEPEK FDVQRNPNSH LAFGFGTHFC LGNQLARLEL SLMTERVLRR
LPDLRLVADD SVLPLRPANF VSGLESMPVV FTPSPPLG


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Related Genes :
[cyp142 cyp142A2 MSMEG_5918] Steroid C26-monooxygenase (EC 1.14.15.28) (Cholest-4-en-3-one C26-monooxygenase) (Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]) (Cholesterol C26-monooxygenase) (Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming]) (Cytochrome P450 142) (Steroid C27-monooxygenase)
[cyp125 cyp125A3 MSMEG_5995] Steroid C26-monooxygenase (EC 1.14.15.29) (Cholest-4-en-3-one C26-monooxygenase) (Cholest-4-en-3-one C26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]) (Cholesterol C26-monooxygenase) (Cholesterol C26-monooxygenase [(25S)-3beta-hydroxycholest-5-en-26-oate forming]) (Cytochrome P450 125) (Steroid C27-monooxygenase)
[CYP27A1 CYP27] Sterol 26-hydroxylase, mitochondrial (EC 1.14.15.15) (5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 26-hydroxylase) (Cytochrome P-450C27/25) (Cytochrome P450 27) (Sterol 27-hydroxylase) (Vitamin D(3) 25-hydroxylase)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[tat] Protein Tat (Transactivating regulatory protein)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[core C PC-C pre-c preC PreC/C preC/C prec/C HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[Cyp7b1] Cytochrome P450 7B1 (24-hydroxycholesterol 7-alpha-hydroxylase) (EC 1.14.14.26) (25/26-hydroxycholesterol 7-alpha-hydroxylase) (EC 1.14.14.29) (3-hydroxysteroid 7-alpha hydroxylase) (Hippocampal transcript 1 protein) (HCT-1) (Oxysterol 7-alpha-hydroxylase)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[CYP7B1] Cytochrome P450 7B1 (24-hydroxycholesterol 7-alpha-hydroxylase) (EC 1.14.14.26) (25/26-hydroxycholesterol 7-alpha-hydroxylase) (EC 1.14.14.29) (3-hydroxysteroid 7-alpha hydroxylase) (Oxysterol 7-alpha-hydroxylase)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[HSD3B7] 3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase) (C(27) 3-beta-HSD) (EC 1.1.1.-) (Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase) (EC 1.1.1.181)
[CYP2C9 CYP2C10] Cytochrome P450 2C9 (EC 1.14.14.1) ((R)-limonene 6-monooxygenase) (EC 1.14.14.53) ((S)-limonene 6-monooxygenase) (EC 1.14.14.51) ((S)-limonene 7-monooxygenase) (EC 1.14.14.52) (CYPIIC9) (Cholesterol 25-hydroxylase) (Cytochrome P-450MP) (Cytochrome P450 MP-4) (Cytochrome P450 MP-8) (Cytochrome P450 PB-1) (S-mephenytoin 4-hydroxylase)
[CYP17A1 CYP17 S17AH] Steroid 17-alpha-hydroxylase/17,20 lyase (EC 1.14.14.19) (17-alpha-hydroxyprogesterone aldolase) (EC 1.14.14.32) (CYPXVII) (Cytochrome P450 17A1) (Cytochrome P450-C17) (Cytochrome P450c17) (Steroid 17-alpha-monooxygenase)
[CYP11B2] Cytochrome P450 11B2, mitochondrial (Aldosterone synthase) (ALDOS) (Aldosterone-synthesizing enzyme) (CYPXIB2) (Corticosterone 18-monooxygenase, CYP11B2) (EC 1.14.15.5) (Cytochrome P-450Aldo) (Cytochrome P-450C18) (Steroid 11-beta-hydroxylase, CYP11B2) (EC 1.14.15.4) (Steroid 18-hydroxylase)
[UL26 AAADCAAH_00030 AOEJBBEJ_00030 BLEONNCJ_00030 BLPDLEPH_00030 DCJDKEDG_00030 DILPLKIK_00030 DJCKHMNK_00030 HMKIDIGP_00030 IPKJLLEP_00030 KINKMKBB_00030 KLEJHFIP_00030 LALCDEHK_00030 NBBNDGNH_00030 NCKHNGOI_00030 NFOBEAPH_00030 OHMFJBFK_00030] Capsid scaffolding protein (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Protease); Assembly protein (Capsid assembly protein)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[Hsd3b7 Cca2] 3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase) (C(27) 3-beta-HSD) (EC 1.1.1.-) (Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase) (EC 1.1.1.181) (Confluent 3Y1 cell-associated 2)
[Hsd3b7] 3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase) (C(27) 3-beta-HSD) (EC 1.1.1.-) (Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase) (EC 1.1.1.181)
[Cyp11b2 Cyp11b-2] Cytochrome P450 11B2, mitochondrial (Aldosterone synthase) (ALDOS) (Aldosterone-synthesizing enzyme) (CYPXIB2) (Corticosterone 18-monooxygenase, CYP11B2) (EC 1.14.15.5) (Cytochrome P-450Aldo) (Cytochrome P-450C18) (Cytochrome P450C11) (Steroid 11-beta-hydroxylase, CYP11B2) (EC 1.14.15.4) (Steroid 18-hydroxylase)
[tat] Protein Tat (Transactivating regulatory protein)

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