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Versicolorin B synthase (EC 4.2.1.143) (5'-oxoaverantin cyclase) (EC 4.2.1.142) (Aflatoxin biosynthesis protein K)

 AFLK_ASPPU              Reviewed;         643 AA.
Q12062; A0A0F0I0N8;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 90.
RecName: Full=Versicolorin B synthase {ECO:0000303|PubMed:8662689};
EC=4.2.1.143 {ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:1731640, ECO:0000269|PubMed:8784203};
AltName: Full=5'-oxoaverantin cyclase {ECO:0000303|PubMed:14602595};
EC=4.2.1.142 {ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:1731640, ECO:0000269|PubMed:8784203};
AltName: Full=Aflatoxin biosynthesis protein K {ECO:0000303|PubMed:15006741};
Flags: Precursor;
Name=aflK {ECO:0000303|PubMed:15006741};
Synonyms=vbs {ECO:0000303|PubMed:8662689}; ORFNames=P875_00052980;
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 /
SU-1).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=1403190;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 163-180
AND 414-428, FUNCTION, AND SUBUNIT.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=8662689; DOI=10.1074/jbc.271.23.13600;
Silva J.C., Minto R.E., Barry C.E., Holland K.A., Townsend C.A.;
"Isolation and characterization of the versicolorin B synthase gene
from Aspergillus parasiticus. Expansion of the aflatoxin b1
biosynthetic gene cluster.";
J. Biol. Chem. 271:13600-13608(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=15094053; DOI=10.1016/S0014-5793(04)00327-8;
Yu J., Bhatnagar D., Cleveland T.E.;
"Completed sequence of aflatoxin pathway gene cluster in Aspergillus
parasiticus.";
FEBS Lett. 564:126-130(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R.,
Ehrlich K.C., Bhatnagar D., Cleveland T.E., Bennett J.W.,
Nierman W.C.;
"Draft genome sequence of Aspergillus parasiticus SU-1.";
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 41-66, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND SUBUNIT.
PubMed=15932995; DOI=10.1128/AEM.71.6.2999-3006.2005;
Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K.,
Nakajima H.;
"Aspergillus parasiticus cyclase catalyzes two dehydration steps in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 71:2999-3006(2005).
[5]
FUNCTION.
PubMed=1339261;
Skory C.D., Chang P.K., Cary J., Linz J.E.;
"Isolation and characterization of a gene from Aspergillus parasiticus
associated with the conversion of versicolorin A to sterigmatocystin
in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 58:3527-3537(1992).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=1731640; DOI=10.1016/0003-9861(92)90366-5;
Lin B.K., Anderson J.A.;
"Purification and properties of versiconal cyclase from Aspergillus
parasiticus.";
Arch. Biochem. Biophys. 293:67-70(1992).
[7]
FUNCTION.
PubMed=8434913;
Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
Ullah A.H.J.;
"Purification of a 40-kilodalton methyltransferase active in the
aflatoxin biosynthetic pathway.";
Appl. Environ. Microbiol. 59:479-484(1993).
[8]
FUNCTION.
PubMed=8368836;
Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: conversion of
norsolorinic acid to averufin.";
Appl. Environ. Microbiol. 59:2486-2492(1993).
[9]
FUNCTION.
PubMed=8368837;
Yabe K., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: cyclase reaction in
the conversion of versiconal to versicolorin B and racemization of
versiconal hemiacetal acetate.";
Appl. Environ. Microbiol. 59:2493-2500(1993).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=8784203; DOI=10.1021/bi960924s;
McGuire S.M., Silva J.C., Casillas E.G., Townsend C.A.;
"Purification and characterization of versicolorin B synthase from
Aspergillus parasiticus. Catalysis of the stereodifferentiating
cyclization in aflatoxin biosynthesis essential to DNA interaction.";
Biochemistry 35:11470-11486(1996).
[11]
GLYCOSYLATION.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=8995367; DOI=10.1074/jbc.272.2.804;
Silva J.C., Townsend C.A.;
"Heterologous expression, isolation, and characterization of
versicolorin B synthase from Aspergillus parasiticus. A key enzyme in
the aflatoxin B1 biosynthetic pathway.";
J. Biol. Chem. 272:804-813(1997).
[12]
FUNCTION.
PubMed=10543813;
Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
"Cloning and characterization of the O-methyltransferase I gene (dmtA)
from Aspergillus parasiticus associated with the conversions of
demethylsterigmatocystin to sterigmatocystin and
dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 65:4987-4994(1999).
[13]
FUNCTION.
PubMed=10584035;
Zhou R., Linz J.E.;
"Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
Aspergillus parasiticus.";
Appl. Environ. Microbiol. 65:5639-5641(1999).
[14]
FUNCTION.
PubMed=11055914; DOI=10.1128/AEM.66.11.4715-4719.2000;
Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G.,
Bhatnagar D., Cleveland T.E.;
"adhA in Aspergillus parasiticus is involved in conversion of 5'-
hydroxyaverantin to averufin.";
Appl. Environ. Microbiol. 66:4715-4719(2000).
[15]
FUNCTION.
PubMed=16256699; DOI=10.1006/bioo.2001.1216;
Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
Townsend C.A.;
"Hexanoate synthase, a specialized type I fatty acid synthase in
aflatoxin B1 biosynthesis.";
Bioorg. Chem. 29:293-307(2001).
[16]
FUNCTION.
PubMed=11996570; DOI=10.1021/ja012185v;
Udwary D.W., Casillas L.K., Townsend C.A.;
"Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
cytochrome P-450 in the final step of aflatoxin biosynthesis.";
J. Am. Chem. Soc. 124:5294-5303(2002).
[17]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
AND SUBCELLULAR LOCATION.
PubMed=14602595; DOI=10.1128/AEM.69.11.6418-6426.2003;
Sakuno E., Yabe K., Nakajima H.;
"Involvement of two cytosolic enzymes and a novel intermediate, 5'-
oxoaverantin, in the pathway from 5'-hydroxyaverantin to averufin in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 69:6418-6426(2003).
[18]
REVIEW, FUNCTION, PATHWAY, AND NOMENCLATURE.
PubMed=15006741; DOI=10.1128/AEM.70.3.1253-1262.2004;
Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D.,
Cleveland T.E., Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
"Clustered pathway genes in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 70:1253-1262(2004).
[19]
FUNCTION.
PubMed=15528514; DOI=10.1128/AEM.70.11.6518-6524.2004;
Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
"Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
formation.";
Appl. Environ. Microbiol. 70:6518-6524(2004).
[20]
FUNCTION.
PubMed=16332900; DOI=10.1128/AEM.71.12.8963-8965.2005;
Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
"An aflatoxin biosynthesis cluster gene encodes a novel oxidase
required for conversion of versicolorin a to sterigmatocystin.";
Appl. Environ. Microbiol. 71:8963-8965(2005).
[21]
FUNCTION.
PubMed=15771506; DOI=10.1021/ja0455188;
Henry K.M., Townsend C.A.;
"Ordering the reductive and cytochrome P450 oxidative steps in
demethylsterigmatocystin formation yields general insights into the
biosynthesis of aflatoxin and related fungal metabolites.";
J. Am. Chem. Soc. 127:3724-3733(2005).
[22]
FUNCTION.
PubMed=16461654; DOI=10.1128/AEM.72.2.1096-1101.2006;
Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
"The aflatoxin biosynthesis cluster gene, aflX, encodes an
oxidoreductase involved in conversion of versicolorin A to
demethylsterigmatocystin.";
Appl. Environ. Microbiol. 72:1096-1101(2006).
[23]
FUNCTION.
PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y.,
Adachi Y., Nakajima H., Yabe K.;
"Involvement of the nadA gene in formation of G-group aflatoxins in
Aspergillus parasiticus.";
Fungal Genet. Biol. 45:1081-1093(2008).
[24]
FUNCTION.
PubMed=18403714; DOI=10.1126/science.1154711;
Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L.,
Kelleher N.L., Townsend C.A.;
"Deconstruction of iterative multidomain polyketide synthase
function.";
Science 320:243-246(2008).
-!- FUNCTION: Versicolorin B synthase; part of the gene cluster that
mediates the biosynthesis of aflatoxins, a group of polyketide-
derived furanocoumarins, and part of the most toxic and
carcinogenic compounds among the known mycotoxins
(PubMed:15006741). The four major aflatoxins produced by
A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2),
aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). The
first step of the pathway is the conversion of acetate to
norsolorinic acid (NOR) and requires the fatty acid synthase
subunits aflA and aflB, as well as the PKS aflC (PubMed:15006741).
AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender
units to synthesize the precursor NOR (PubMed:18403714). The
hexanoyl starter unit is provided to the acyl-carrier protein
(ACP) domain by the fungal fatty acid synthase aflA/aflB
(PubMed:16256699). The second step is the conversion of NOR to
averantin (AVN) and requires the norsolorinic acid ketoreductase
aflD, which catalyzes the dehydration of norsolorinic acid to form
(1'S)-averantin (PubMed:10584035). The norsolorinic acid
reductases aflE and aflF may also play a role in the conversion of
NOR to AVN (PubMed:15006741). The cytochrome P450 monooxygenase
aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin
(HAVN) (PubMed:8368836). The next step is performed by the 5'-
hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-
oxoaverantin (OAVN) which is further converted to averufin (AVF)
by aflK that plays a dual role in the pathway, as a 5'-
oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin,
as well as a versicolorin B synthase in a later step in the
pathway (PubMed:15006741, PubMed:11055914, PubMed:15932995). The
averufin oxidase aflI catalyzes the conversion of AVF to
versiconal hemiacetal acetate (VHA) (PubMed:15006741). VHA is then
the substrate for the versiconal hemiacetal acetate esterase aflJ
to yield versiconal (VAL) (PubMed:15006741). Versicolorin B
synthase aflK then converts VAL to versicolorin B (VERB) by
closing the bisfuran ring of aflatoxin which is required for DNA-
binding, thus giving to aflatoxin its activity as a mutagen
(PubMed:8662689, PubMed:15932995, PubMed:1731640, PubMed:8368837,
PubMed:8784203, PubMed:14602595, PubMed:15006741). Then, the
activity of the versicolorin B desaturase aflL leads to
versicolorin A (VERA) (PubMed:15006741, PubMed:8368837). A branch
point starts from VERB since it can also be converted to
dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL,
VERA being a precursor for aflatoxins B1 and G1, and DMDHST for
aflatoxins B2 and G2 (PubMed:15006741). Next, the versicolorin
reductase aflM and the cytochrome P450 monooxygenase aflN are
involved in conversion of VERA to demethylsterigmatocystin (DMST)
(PubMed:15006741, PubMed:1339261, PubMed:15771506). AflX and aflY
seem also involved in this step, through probable aflX-mediated
epoxide ring-opening step following versicolorin A oxidation and
aflY-mediated Baeyer-Villiger oxidation required for the formation
of the xanthone ring (PubMed:16332900, PubMed:16461654). The
methyltransferase aflO then leads to the modification of DMST to
sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin
(DHST) (PubMed:10543813). Both ST and DHST are then substrates of
the O-methyltransferase aflP to yield O-methylsterigmatocystin
(OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively
(PubMed:8434913). Finally OMST is converted to aflatoxins B1 and
G1, and DHOMST to aflatoxins B2 and G2, via the action of several
enzymes including O-methylsterigmatocystin oxidoreductase aflQ,
the cytodhrome P450 monooxygenase aflU, but also the NADH-
dependent flavin oxidoreductase nadA which is specifically
required for the synthesis of AFG1 (PubMed:15006741,
PubMed:11996570, PubMed:15528514, PubMed:18486503).
{ECO:0000269|PubMed:10543813, ECO:0000269|PubMed:10584035,
ECO:0000269|PubMed:11055914, ECO:0000269|PubMed:11996570,
ECO:0000269|PubMed:1339261, ECO:0000269|PubMed:14602595,
ECO:0000269|PubMed:15006741, ECO:0000269|PubMed:15528514,
ECO:0000269|PubMed:15771506, ECO:0000269|PubMed:15932995,
ECO:0000269|PubMed:16256699, ECO:0000269|PubMed:16332900,
ECO:0000269|PubMed:16461654, ECO:0000269|PubMed:1731640,
ECO:0000269|PubMed:18403714, ECO:0000269|PubMed:18486503,
ECO:0000269|PubMed:8368836, ECO:0000269|PubMed:8368837,
ECO:0000269|PubMed:8434913, ECO:0000269|PubMed:8662689,
ECO:0000269|PubMed:8784203, ECO:0000305|PubMed:15006741}.
-!- CATALYTIC ACTIVITY: Versiconal = versicolorin B + H(2)O.
{ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:15932995,
ECO:0000269|PubMed:1731640, ECO:0000269|PubMed:8784203}.
-!- CATALYTIC ACTIVITY: 5'-oxoaverantin = (1'S,5'S)-averufin + H(2)O.
{ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:15932995,
ECO:0000269|PubMed:1731640, ECO:0000269|PubMed:8784203}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:E4QP00};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=20 uM for 5'-oxoaverantin {ECO:0000269|PubMed:14602595,
ECO:0000269|PubMed:1731640};
KM=3.1 uM for versiconal (at pH 6.0 and 30 degrees Celsius)
{ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:1731640};
Vmax=6.67 nmol/min/mg enzyme with 5'-oxoaverantin as substrate
{ECO:0000269|PubMed:14602595, ECO:0000269|PubMed:1731640};
Vmax=0.15 umol/min/mg enzyme with versiconal (at pH 6.0 and 30
degrees Celsius) as substrate {ECO:0000269|PubMed:14602595,
ECO:0000269|PubMed:1731640};
pH dependence:
Optimum pH is 5.5. {ECO:0000269|PubMed:14602595,
ECO:0000269|PubMed:1731640};
-!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
{ECO:0000269|PubMed:15094053, ECO:0000305|PubMed:15006741}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14602595,
ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:8662689,
ECO:0000269|PubMed:8784203}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:14602595, ECO:0000305|PubMed:15932995}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:8995367}.
-!- SIMILARITY: Belongs to the GMC oxidoreductase family.
{ECO:0000305}.
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EMBL; U51327; AAC49318.1; -; Genomic_DNA.
EMBL; U51328; AAC49319.1; -; mRNA.
EMBL; AY371490; AAS66012.1; -; Genomic_DNA.
EMBL; JZEE01000729; KJK60751.1; -; Genomic_DNA.
ProteinModelPortal; Q12062; -.
CAZy; AA3; Auxiliary Activities 3.
EnsemblFungi; KJK60751; KJK60751; P875_00052980.
KEGG; ag:AAC49318; -.
KO; K17646; -.
BioCyc; MetaCyc:MONOMER-14040; -.
BRENDA; 4.2.1.142; 523.
BRENDA; 4.2.1.143; 523.
UniPathway; UPA00287; -.
Proteomes; UP000033540; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0045122; P:aflatoxin biosynthetic process; IDA:UniProtKB.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR012132; GMC_OxRdtase.
InterPro; IPR000172; GMC_OxRdtase_N.
InterPro; IPR007867; GMC_OxRtase_C.
Pfam; PF05199; GMC_oxred_C; 1.
Pfam; PF00732; GMC_oxred_N; 1.
PIRSF; PIRSF000137; Alcohol_oxidase; 1.
SUPFAM; SSF51905; SSF51905; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; FAD;
Flavoprotein; Glycoprotein; Lyase; Reference proteome.
PROPEP 1 41 {ECO:0000269|PubMed:15932995}.
/FTId=PRO_0000424163.
CHAIN 22 643 Versicolorin B synthase.
/FTId=PRO_0000424164.
NP_BIND 84 85 FAD. {ECO:0000250|UniProtKB:E4QP00}.
NP_BIND 105 106 FAD. {ECO:0000250|UniProtKB:E4QP00}.
NP_BIND 171 174 FAD. {ECO:0000250|UniProtKB:E4QP00}.
NP_BIND 624 625 FAD. {ECO:0000250|UniProtKB:E4QP00}.
BINDING 613 613 FAD; via amide nitrogen.
{ECO:0000250|UniProtKB:E4QP00}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 507 507 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 643 AA; 70271 MW; 4B903BA6A0F39D11 CRC64;
MGRNWFQVTA MAVVPVVGIM AAVNPTILSS AASSLPSLGA MFTSDDFASQ MDGRIQAQGL
LSSHFGMYGW PGQSFDYVIV GGGTAGLAMA RRLSQDGTAS VAVIEAGGFY ETDAGNATEV
PMYLFNYFFD NGKVKNPLFD WYQYTTPQPG LAQREMFYMQ GKTLGGSTAR GAMLYHRGSK
GAYDMWADHV GDDSYRWDKW LPYFQKSVHF SGPETNPRPA NATALNDNTA FTASGGPVHV
GYPFQVNAIS SWVDRALAKM GFPEAQGFSN GNLLGRSYIT HTINPYTRRR ETASSSYLRE
ALMESNNLNI FTRTLVKRVL FDDQNRATGV TVNTDGFEWQ IGARKEVILS AGVMRSPQLL
MVSGIGPKDH LEQLGIPVRS DLSGVGQNMQ DTIILGPTVP VKVESHSQLM GNKETLPRAI
REYNEQRKGL LTNPGQDYFA FEKHQPGMLK ESTAADIDAA FPDDWPTFSY IALDDTFVPQ
YDGKNYFSMS AALMTPFSRG TVTINSNDTA NPPIVDPQWL ADPRDQEMAV AAFRRCREIV
ASDVMREVVA GPEILPGPQY QTDEEILNYI AETSDAYYAG VGTCAMGKAD DPKAVVDSKA
RVLGVKGLRI VDASIFPFAI DGQPMGTVYA LAEKIAAEMM AGQ


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CSB-EL014703BO Bovine Molybdenum cofactor biosynthesis protein 1 [Includes: Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit 96T
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CSB-EL014703HU Human Molybdenum cofactor biosynthesis protein 1 [Includes: Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit 96T
U1898h CLIA 2,3-epoxysqualene--lanosterol cyclase,Homo sapiens,hOSC,Human,Lanosterol synthase,LSS,OSC,OSC,Oxidosqualene--lanosterol cyclase 96T
U1898h CLIA kit 2,3-epoxysqualene--lanosterol cyclase,Homo sapiens,hOSC,Human,Lanosterol synthase,LSS,OSC,OSC,Oxidosqualene--lanosterol cyclase 96T
E1898h ELISA kit 2,3-epoxysqualene--lanosterol cyclase,Homo sapiens,hOSC,Human,Lanosterol synthase,LSS,OSC,OSC,Oxidosqualene--lanosterol cyclase 96T
E1898h ELISA 2,3-epoxysqualene--lanosterol cyclase,Homo sapiens,hOSC,Human,Lanosterol synthase,LSS,OSC,OSC,Oxidosqualene--lanosterol cyclase 96T
E1898b ELISA 2,3-epoxysqualene--lanosterol cyclase,Bos taurus,Bovine,Lanosterol synthase,LSS,OSC,Oxidosqualene--lanosterol cyclase 96T
E1898r ELISA kit 2,3-epoxysqualene--lanosterol cyclase,Lanosterol synthase,Lss,OSC,Osc,Oxidosqualene--lanosterol cyclase,Rat,Rattus norvegicus 96T
E1898m ELISA kit 2,3-epoxysqualene--lanosterol cyclase,Lanosterol synthase,Lss,Mouse,Mus musculus,OSC,Oxidosqualene--lanosterol cyclase 96T
U1898r CLIA 2,3-epoxysqualene--lanosterol cyclase,Lanosterol synthase,Lss,OSC,Osc,Oxidosqualene--lanosterol cyclase,Rat,Rattus norvegicus 96T
E1898b ELISA kit 2,3-epoxysqualene--lanosterol cyclase,Bos taurus,Bovine,Lanosterol synthase,LSS,OSC,Oxidosqualene--lanosterol cyclase 96T
U1898r CLIA kit 2,3-epoxysqualene--lanosterol cyclase,Lanosterol synthase,Lss,OSC,Osc,Oxidosqualene--lanosterol cyclase,Rat,Rattus norvegicus 96T


 

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