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Mycocyclosin synthase (EC 1.14.21.9) (Cytochrome P450 121) (Cytochrome P450 MT2)

 CP121_MYCTU             Reviewed;         396 AA.
P9WPP7; L0TAQ4; P0A514; Q59571;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
05-DEC-2018, entry version 34.
RecName: Full=Mycocyclosin synthase;
EC=1.14.19.70 {ECO:0000269|PubMed:19416919};
AltName: Full=Cytochrome P450 121;
AltName: Full=Cytochrome P450 MT2;
Name=cyp121; OrderedLocusNames=Rv2276; ORFNames=MTCY339.34c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
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).
[2]
FUNCTION.
Souter A., McLean K.J., Smith W.E., Munro A.W.;
"The genome sequence of Mycobacterium tuberculosis reveals cytochromes
P450 as novel anti-TB drug targets.";
J. Chem. Technol. Biotechnol. 75:933-941(2000).
[3]
FUNCTION, COFACTOR, CIRCULAR DICHROISM ANALYSIS, EPR SPECTROSCOPY,
MAGNETIC CIRCULAR DICHROISM, MASS SPECTROMETRY, AND RESONANCE RAMAN
SPECTROSCOPY.
PubMed=12237220; DOI=10.1016/S0162-0134(02)00479-8;
McLean K.J., Cheesman M.R., Rivers S.L., Richmond A., Leys D.,
Chapman S.K., Reid G.A., Price N.C., Kelly S.M., Clarkson J.,
Smith W.E., Munro A.W.;
"Expression, purification and spectroscopic characterization of the
cytochrome P450 CYP121 from Mycobacterium tuberculosis.";
J. Inorg. Biochem. 91:527-541(2002).
[4]
CRYSTALLIZATION.
PubMed=11914502; DOI=10.1107/S0907444902002676;
Mowat C.G., Leys D., McLean K.J., Rivers S.L., Richmond A.,
Munro A.W., Ortiz Lombardia M., Alzari P.M., Reid G.A., Chapman S.K.,
Walkinshaw M.D.;
"Crystallization and preliminary crystallographic analysis of a novel
cytochrome P450 from Mycobacterium tuberculosis.";
Acta Crystallogr. D 58:704-705(2002).
[5]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[6]
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).
[7]
X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS) IN COMPLEX WITH HEME, AND
COFACTOR.
PubMed=12435731; DOI=10.1074/jbc.M209928200;
Leys D., Mowat C.G., McLean K.J., Richmond A., Chapman S.K.,
Walkinshaw M.D., Munro A.W.;
"Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A
reveals novel features of cytochrome P450.";
J. Biol. Chem. 278:5141-5147(2003).
[8]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH HEME AND
SUBSTRATE, AND COFACTOR.
PubMed=17028183; DOI=10.1074/jbc.M607665200;
Seward H.E., Roujeinikova A., McLean K.J., Munro A.W., Leys D.;
"Crystal structure of the Mycobacterium tuberculosis P450 CYP121-
fluconazole complex reveals new azole drug-P450 binding mode.";
J. Biol. Chem. 281:39437-39443(2006).
[9]
X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF MUTANTS IN COMPLEX WITH
HEME, MUTAGENESIS OF ALA-233; SER-237; SER-279; PHE-338; PRO-346 AND
ARG-386, COFACTOR, AND ACTIVITY REGULATION.
PubMed=18818197; DOI=10.1074/jbc.M802115200;
McLean K.J., Carroll P., Lewis D.G., Dunford A.J., Seward H.E.,
Neeli R., Cheesman M.R., Marsollier L., Douglas P., Smith W.E.,
Rosenkrands I., Cole S.T., Leys D., Parish T., Munro A.W.;
"Characterization of active site structure in CYP121. A cytochrome
P450 essential for viability of Mycobacterium tuberculosis H37Rv.";
J. Biol. Chem. 283:33406-33416(2008).
[10]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH HEME AND
SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, REACTION MECHANISM, AND COFACTOR.
PubMed=19416919; DOI=10.1073/pnas.0812191106;
Belin P., Le Du M.H., Fielding A., Lequin O., Jacquet M.,
Charbonnier J.B., Lecoq A., Thai R., Courcon M., Masson C., Dugave C.,
Genet R., Pernodet J.L., Gondry M.;
"Identification and structural basis of the reaction catalyzed by
CYP121, an essential cytochrome P450 in Mycobacterium tuberculosis.";
Proc. Natl. Acad. Sci. U.S.A. 106:7426-7431(2009).
[11]
X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) IN COMPLEX WITH HEME AND
SUBSTRATE ANALOGS, AND COFACTOR.
PubMed=22890978; DOI=10.1002/anie.201202544;
Hudson S.A., McLean K.J., Surade S., Yang Y.Q., Leys D., Ciulli A.,
Munro A.W., Abell C.;
"Application of fragment screening and merging to the discovery of
inhibitors of the Mycobacterium tuberculosis cytochrome P450 CYP121.";
Angew. Chem. Int. Ed. Engl. 51:9311-9316(2012).
[12]
X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 2-396 IN COMPLEX WITH HEME
AND SUBSTRATE ANALOGS, SUBSTRATE SPECIFICITY, AND COFACTOR.
PubMed=23620594; DOI=10.1074/jbc.M112.443853;
Fonvielle M., Le Du M.H., Lequin O., Lecoq A., Jacquet M., Thai R.,
Dubois S., Grach G., Gondry M., Belin P.;
"Substrate and reaction specificity of Mycobacterium tuberculosis
cytochrome P450 CYP121: insights from biochemical studies and crystal
structures.";
J. Biol. Chem. 288:17347-17359(2013).
-!- FUNCTION: Catalyzes C-C bond formation between the carbons ortho
to the phenolic hydroxyl of cyclo(L-tyr-L-tyr) (cYY) producing
mycocyclosin. Can also use cyclo(L-Tyr-L-Phe) (cYF), cyclo(L-Tyr-
L-Trp) (cYW) and cyclo(L-Tyr-L-3,4-dihydroxyphenylalanine) (cY-
DOPA) as substrate. {ECO:0000269|PubMed:12237220,
ECO:0000269|PubMed:19416919, ECO:0000269|Ref.2}.
-!- CATALYTIC ACTIVITY:
Reaction=cyclo(L-tyrosyl-L-tyrosyl) + 2 H(+) + O2 + 2 reduced
[2Fe-2S]-[ferredoxin] = 2 H2O + mycoclysin + 2 oxidized [2Fe-
2S]-[ferredoxin]; Xref=Rhea:RHEA:35547, Rhea:RHEA-COMP:10000,
Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:65063, ChEBI:CHEBI:71596; EC=1.14.19.70;
Evidence={ECO:0000269|PubMed:19416919};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:12237220,
ECO:0000269|PubMed:12435731, ECO:0000269|PubMed:17028183,
ECO:0000269|PubMed:18818197, ECO:0000269|PubMed:19416919,
ECO:0000269|PubMed:22890978, ECO:0000269|PubMed:23620594};
-!- ACTIVITY REGULATION: Inhibited by clotrimazole, econazole,
ketoconazole, and miconazole. {ECO:0000269|PubMed:18818197}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=21.3 uM for cYY (at pH7.2 and 30 degrees Celsius)
{ECO:0000269|PubMed:19416919};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=43128; Method=Electrospray; Range=2-396;
Evidence={ECO:0000269|PubMed:12237220};
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; AL123456; CCP45058.1; -; Genomic_DNA.
PIR; H70730; H70730.
RefSeq; NP_216792.1; NC_000962.3.
RefSeq; WP_003411685.1; NZ_NVQJ01000008.1.
PDB; 1N40; X-ray; 1.06 A; A=1-396.
PDB; 1N4G; X-ray; 1.80 A; A=1-396.
PDB; 2IJ5; X-ray; 1.60 A; A/B/C/D/E/F=1-396.
PDB; 2IJ7; X-ray; 1.90 A; A/B/C/D/E/F=1-396.
PDB; 3CXV; X-ray; 1.70 A; A=1-396.
PDB; 3CXX; X-ray; 1.90 A; A=1-396.
PDB; 3CXY; X-ray; 1.45 A; A=1-396.
PDB; 3CXZ; X-ray; 1.08 A; A=1-396.
PDB; 3CY0; X-ray; 1.90 A; A=1-396.
PDB; 3CY1; X-ray; 1.75 A; A=1-396.
PDB; 3G5F; X-ray; 1.40 A; A=1-396.
PDB; 3G5H; X-ray; 1.40 A; A=1-396.
PDB; 4G1X; X-ray; 1.30 A; A=2-396.
PDB; 4G2G; X-ray; 2.25 A; A=2-396.
PDB; 4G44; X-ray; 1.24 A; A=1-396.
PDB; 4G45; X-ray; 1.53 A; A=1-396.
PDB; 4G46; X-ray; 1.52 A; A=1-396.
PDB; 4G47; X-ray; 1.34 A; A=1-396.
PDB; 4G48; X-ray; 1.50 A; A=1-396.
PDB; 4ICT; X-ray; 1.80 A; A=3-396.
PDB; 4IPS; X-ray; 1.20 A; A=2-396.
PDB; 4IPW; X-ray; 1.40 A; A=2-396.
PDB; 4IQ7; X-ray; 1.90 A; A=2-396.
PDB; 4IQ9; X-ray; 1.40 A; A=2-396.
PDB; 5IBD; X-ray; 1.77 A; A=1-396.
PDB; 5IBE; X-ray; 1.62 A; A=1-396.
PDB; 5IBF; X-ray; 1.70 A; A=1-396.
PDB; 5IBG; X-ray; 2.10 A; A=1-396.
PDB; 5IBH; X-ray; 2.02 A; A=1-396.
PDB; 5IBI; X-ray; 2.20 A; A=1-396.
PDB; 5IBJ; X-ray; 2.50 A; A=1-396.
PDB; 5OP9; X-ray; 1.46 A; A=1-396.
PDBsum; 1N40; -.
PDBsum; 1N4G; -.
PDBsum; 2IJ5; -.
PDBsum; 2IJ7; -.
PDBsum; 3CXV; -.
PDBsum; 3CXX; -.
PDBsum; 3CXY; -.
PDBsum; 3CXZ; -.
PDBsum; 3CY0; -.
PDBsum; 3CY1; -.
PDBsum; 3G5F; -.
PDBsum; 3G5H; -.
PDBsum; 4G1X; -.
PDBsum; 4G2G; -.
PDBsum; 4G44; -.
PDBsum; 4G45; -.
PDBsum; 4G46; -.
PDBsum; 4G47; -.
PDBsum; 4G48; -.
PDBsum; 4ICT; -.
PDBsum; 4IPS; -.
PDBsum; 4IPW; -.
PDBsum; 4IQ7; -.
PDBsum; 4IQ9; -.
PDBsum; 5IBD; -.
PDBsum; 5IBE; -.
PDBsum; 5IBF; -.
PDBsum; 5IBG; -.
PDBsum; 5IBH; -.
PDBsum; 5IBI; -.
PDBsum; 5IBJ; -.
PDBsum; 5OP9; -.
ProteinModelPortal; P9WPP7; -.
SMR; P9WPP7; -.
STRING; 83332.Rv2276; -.
BindingDB; P9WPP7; -.
ChEMBL; CHEMBL1681615; -.
PaxDb; P9WPP7; -.
PRIDE; P9WPP7; -.
EnsemblBacteria; CCP45058; CCP45058; Rv2276.
GeneID; 888373; -.
KEGG; mtu:Rv2276; -.
TubercuList; Rv2276; -.
eggNOG; ENOG4106NM8; Bacteria.
eggNOG; ENOG410YRWJ; LUCA.
KO; K17483; -.
OMA; PRDDMID; -.
PhylomeDB; P9WPP7; -.
BioCyc; MetaCyc:G185E-6494-MONOMER; -.
PRO; PR:P9WPP7; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070025; F:carbon monoxide binding; IDA:MTBBASE.
GO; GO:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; IBA:GO_Central.
GO; GO:0009975; F:cyclase activity; IDA:MTBBASE.
GO; GO:0020037; F:heme binding; IDA:MTBBASE.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; IDA:MTBBASE.
GO; GO:0046996; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, with NAD(P)H as one donor, and the other dehydrogenated; IDA:UniProtKB.
GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
GO; GO:0006707; P:cholesterol catabolic process; IBA:GO_Central.
GO; GO:0055114; P:oxidation-reduction process; IMP:MTBBASE.
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.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Heme; Iron; Metal-binding;
Monooxygenase; Oxidoreductase; Reference proteome.
CHAIN 1 396 Mycocyclosin synthase.
/FTId=PRO_0000052274.
REGION 85 86 Substrate binding.
METAL 345 345 Iron (heme axial ligand).
BINDING 77 77 Substrate. {ECO:0000269|PubMed:17028183,
ECO:0000269|PubMed:19416919}.
BINDING 237 237 Substrate. {ECO:0000269|PubMed:17028183,
ECO:0000269|PubMed:19416919}.
BINDING 286 286 Heme. {ECO:0000269|PubMed:12435731,
ECO:0000269|PubMed:17028183,
ECO:0000269|PubMed:18818197,
ECO:0000269|PubMed:19416919,
ECO:0000269|PubMed:22890978,
ECO:0000269|PubMed:23620594}.
BINDING 301 301 Substrate. {ECO:0000269|PubMed:17028183,
ECO:0000269|PubMed:19416919}.
BINDING 343 343 Heme. {ECO:0000269|PubMed:12435731,
ECO:0000269|PubMed:17028183,
ECO:0000269|PubMed:18818197,
ECO:0000269|PubMed:19416919,
ECO:0000269|PubMed:22890978,
ECO:0000269|PubMed:23620594}.
BINDING 385 385 Substrate. {ECO:0000269|PubMed:17028183,
ECO:0000269|PubMed:19416919}.
SITE 168 168 Participates in a stacking interactions
with the tyrosyl of cYY.
SITE 182 182 Participates in a stacking interactions
with the tyrosyl of cYY.
SITE 346 346 Important for the position of heme.
MUTAGEN 233 233 A->G: Has little effect on the heme
conformation but significantly alters the
environment of the heme and the affinity
for azoles.
{ECO:0000269|PubMed:18818197}.
MUTAGEN 237 237 S->A: Has little effect on the heme
conformation but significantly alters the
environment of the heme and the affinity
for azoles.
{ECO:0000269|PubMed:18818197}.
MUTAGEN 279 279 S->A: Has little effect.
{ECO:0000269|PubMed:18818197}.
MUTAGEN 338 338 F->H: No significant change.
{ECO:0000269|PubMed:18818197}.
MUTAGEN 346 346 P->I: Considerable effects on the heme
macrocycle conformation. Mutant leads to
a more planar heme conformation.
{ECO:0000269|PubMed:18818197}.
MUTAGEN 386 386 R->I: No significant change.
{ECO:0000269|PubMed:18818197}.
STRAND 7 9 {ECO:0000244|PDB:2IJ5}.
STRAND 15 17 {ECO:0000244|PDB:1N40}.
HELIX 20 28 {ECO:0000244|PDB:1N40}.
STRAND 30 35 {ECO:0000244|PDB:1N40}.
STRAND 41 45 {ECO:0000244|PDB:1N40}.
HELIX 48 55 {ECO:0000244|PDB:1N40}.
STRAND 60 62 {ECO:0000244|PDB:1N40}.
HELIX 63 66 {ECO:0000244|PDB:1N40}.
HELIX 80 84 {ECO:0000244|PDB:1N40}.
HELIX 85 91 {ECO:0000244|PDB:1N40}.
HELIX 95 101 {ECO:0000244|PDB:1N40}.
HELIX 109 127 {ECO:0000244|PDB:1N40}.
STRAND 129 132 {ECO:0000244|PDB:5IBH}.
TURN 133 137 {ECO:0000244|PDB:1N40}.
HELIX 138 150 {ECO:0000244|PDB:1N40}.
HELIX 154 156 {ECO:0000244|PDB:1N40}.
HELIX 157 162 {ECO:0000244|PDB:1N40}.
HELIX 164 167 {ECO:0000244|PDB:1N40}.
HELIX 176 194 {ECO:0000244|PDB:1N40}.
HELIX 201 210 {ECO:0000244|PDB:1N40}.
HELIX 213 215 {ECO:0000244|PDB:1N40}.
HELIX 220 250 {ECO:0000244|PDB:1N40}.
HELIX 253 261 {ECO:0000244|PDB:1N40}.
HELIX 263 265 {ECO:0000244|PDB:1N40}.
HELIX 266 275 {ECO:0000244|PDB:1N40}.
STRAND 280 282 {ECO:0000244|PDB:2IJ7}.
STRAND 284 290 {ECO:0000244|PDB:1N40}.
STRAND 292 294 {ECO:0000244|PDB:1N40}.
STRAND 297 299 {ECO:0000244|PDB:1N40}.
STRAND 304 307 {ECO:0000244|PDB:1N40}.
HELIX 309 313 {ECO:0000244|PDB:1N40}.
TURN 316 318 {ECO:0000244|PDB:1N40}.
STRAND 319 321 {ECO:0000244|PDB:1N40}.
HELIX 341 343 {ECO:0000244|PDB:1N40}.
HELIX 348 365 {ECO:0000244|PDB:1N40}.
STRAND 370 373 {ECO:0000244|PDB:1N40}.
HELIX 375 377 {ECO:0000244|PDB:1N40}.
STRAND 383 386 {ECO:0000244|PDB:1N40}.
STRAND 393 395 {ECO:0000244|PDB:1N40}.
SEQUENCE 396 AA; 43256 MW; 510C3B638419DCCB CRC64;
MTATVLLEVP FSARGDRIPD AVAELRTREP IRKVRTITGA EAWLVSSYAL CTQVLEDRRF
SMKETAAAGA PRLNALTVPP EVVNNMGNIA DAGLRKAVMK AITPKAPGLE QFLRDTANSL
LDNLITEGAP ADLRNDFADP LATALHCKVL GIPQEDGPKL FRSLSIAFMS SADPIPAAKI
NWDRDIEYMA GILENPNITT GLMGELSRLR KDPAYSHVSD ELFATIGVTF FGAGVISTGS
FLTTALISLI QRPQLRNLLH EKPELIPAGV EELLRINLSF ADGLPRLATA DIQVGDVLVR
KGELVLVLLE GANFDPEHFP NPGSIELDRP NPTSHLAFGR GQHFCPGSAL GRRHAQIGIE
ALLKKMPGVD LAVPIDQLVW RTRFQRRIPE RLPVLW


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EIAAB08934 Cyp2d1,Cyp2d-1,Cyp2d9,CYPIID1,Cytochrome P450 2D1,Cytochrome P450-CMF1A,Cytochrome P450-DB1,Cytochrome P450-UT-7,Debrisoquine 4-hydroxylase,Rat,Rattus norvegicus
EIAAB08904 CYP2B4,CYPIIB4,Cytochrome P450 2B4,Cytochrome P450 isozyme 2,Cytochrome P450 LM2,Cytochrome P450 type B0,Cytochrome P450 type B1,Oryctolagus cuniculus,Rabbit
EIAAB08908 Cyp2b10,Cyp2b-10,Cyp2b20,CYPIIB10,CYPIIB20,Cytochrome P450 2B10,Cytochrome P450 2B20,Cytochrome P450 clone PF3_46,Cytochrome P450-16-alpha,Mouse,Mus musculus,P24,Testosterone 16-alpha hydroxylase
EIAAB08847 CYP1A2,CYPIA2,Cytochrome P450 1A2,Cytochrome P450 isozyme 4,Cytochrome P450 LM4,Cytochrome P450-PM4,Oryctolagus cuniculus,Rabbit
EIAAB08843 CYP1A1,CYPIA1,Cytochrome P450 1A1,Cytochrome P450 form 6,Cytochrome P450-C,Cytochrome P450-P1,Homo sapiens,Human
U1557m CLIA 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
E1557m ELISA 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
E1557m ELISA kit 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
E1557r ELISA kit 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T
E1557p ELISA kit 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
E1557b ELISA kit 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T
U1557b CLIA 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T
EIAAB08924 Cyp2c13,Cyp2c-13,CYPIIC13,Cytochrome P450 2C13, male-specific,Cytochrome P-450g,Cytochrome P450-G,Cytochrome P450-UT-5,Rat,Rattus norvegicus
U1557p CLIA 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
U1557r CLIA 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T


 

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