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Fatty acid synthase beta subunit aflB (EC 2.3.1.86) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39); S-acyl fatty acid synthase thioesterase (EC 3.1.2.14) (Aflatoxin biosynthesis protein B)]

 AFLB_ASPPU              Reviewed;        1888 AA.
Q8TGA1; A0A0F0I0T2;
30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
10-MAY-2017, entry version 69.
RecName: Full=Fatty acid synthase beta subunit aflB {ECO:0000303|PubMed:16256699};
EC=2.3.1.86 {ECO:0000305|PubMed:16256699};
Includes:
RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000305|PubMed:16256699};
EC=4.2.1.59 {ECO:0000305|PubMed:16256699};
Includes:
RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000305|PubMed:16256699};
EC=1.3.1.9 {ECO:0000305|PubMed:16256699};
Includes:
RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000305|PubMed:16256699};
EC=2.3.1.38 {ECO:0000305|PubMed:16256699};
Includes:
RecName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000305|PubMed:16256699};
EC=2.3.1.39 {ECO:0000305|PubMed:16256699};
Includes:
RecName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000305|PubMed:16256699};
EC=3.1.2.14 {ECO:0000305|PubMed:16256699};
AltName: Full=Aflatoxin biosynthesis protein B {ECO:0000303|PubMed:15006741};
Name=aflB {ECO:0000303|PubMed:15006741};
Synonyms=fas-1 {ECO:0000303|PubMed:15094053},
fas-1A {ECO:0000303|PubMed:8572694},
uvm8 {ECO:0000303|PubMed:8572694}; ORFNames=P875_00052979;
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], FUNCTION, AND PATHWAY.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND
NOMENCLATURE.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, 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).
[4]
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.
[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.
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).
[7]
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).
[8]
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).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8572694;
Mahanti N., Bhatnagar D., Cary J.W., Joubran J., Linz J.E.;
"Structure and function of fas-1A, a gene encoding a putative fatty
acid synthetase directly involved in aflatoxin biosynthesis in
Aspergillus parasiticus.";
Appl. Environ. Microbiol. 62:191-195(1996).
[10]
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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
FUNCTION.
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
INDUCTION.
PubMed=23281343; DOI=10.1002/mbo3.63;
Hong S.Y., Roze L.V., Wee J., Linz J.E.;
"Evidence that a transcription factor regulatory network coordinates
oxidative stress response and secondary metabolism in aspergilli.";
MicrobiologyOpen 2:144-160(2013).
-!- FUNCTION: Fatty acid synthase beta subunit; 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,
PubMed:15094053). 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, PubMed:8572694). 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:15006741, PubMed:8368837, PubMed:15932995). 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:15528514,
ECO:0000269|PubMed:15771506, ECO:0000269|PubMed:15932995,
ECO:0000269|PubMed:16256699, ECO:0000269|PubMed:16332900,
ECO:0000269|PubMed:16461654, ECO:0000269|PubMed:18403714,
ECO:0000269|PubMed:18486503, ECO:0000269|PubMed:8368836,
ECO:0000269|PubMed:8368837, ECO:0000269|PubMed:8434913,
ECO:0000269|PubMed:8572694, ECO:0000305|PubMed:15006741,
ECO:0000305|PubMed:15094053}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-
chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
{ECO:0000305|PubMed:16256699}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [acyl-carrier-protein] = CoA +
acetyl-[acyl-carrier-protein]. {ECO:0000305|PubMed:16256699}.
-!- CATALYTIC ACTIVITY: Malonyl-CoA + an [acyl-carrier-protein] = CoA
+ a malonyl-[acyl-carrier-protein]. {ECO:0000305|PubMed:16256699}.
-!- CATALYTIC ACTIVITY: A (3R)-3-hydroxyacyl-[acyl-carrier protein] =
a trans-2-enoyl-[acyl-carrier protein] + H(2)O.
{ECO:0000305|PubMed:16256699}.
-!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.
{ECO:0000305|PubMed:16256699}.
-!- CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-
carrier-protein] + oleate. {ECO:0000305|PubMed:16256699}.
-!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
{ECO:0000269|PubMed:15006741, ECO:0000269|PubMed:15094053,
ECO:0000269|PubMed:16256699}.
-!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional
subunits (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
-!- INDUCTION: Expression is regulated by the atfB, srrA, AP-1, and
msnA transcription regulators (PubMed:23281343). These factors
bind respectively to the conserved motifs CRE1 (5'-TGACATAA-3'),
SRRA (5'-T/GNT/CAAGCCNNG/AA/GC/ANT/C-3'), AP-1 (5'-TGAGTAC-3') and
STRE (5'-CCCCT-3'), present in the promoter of aflB
(PubMed:23281343). {ECO:0000269|PubMed:23281343}.
-!- DISRUPTION PHENOTYPE: Abolishes the production of norsolorinic
acid and aflatoxin B1 (PubMed:8572694).
{ECO:0000269|PubMed:8572694}.
-!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit
beta family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=KJK60796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF391094; AAL99899.1; -; Genomic_DNA.
EMBL; AY371490; AAS66003.1; -; Genomic_DNA.
EMBL; JZEE01000728; KJK60796.1; ALT_SEQ; Genomic_DNA.
ProteinModelPortal; Q8TGA1; -.
SMR; Q8TGA1; -.
EnsemblFungi; KJK60796; KJK60796; P875_00052979.
UniPathway; UPA00287; -.
Proteomes; UP000033540; Unassembled WGS sequence.
GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR013565; DUF1729.
InterPro; IPR003965; Fatty_acid_synthase.
InterPro; IPR016452; Fatty_acid_Synthase_bsu_fun.
InterPro; IPR029069; HotDog_dom.
InterPro; IPR002539; MaoC_dom.
InterPro; IPR020801; PKS_acyl_transferase.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF08354; DUF1729; 1.
Pfam; PF01575; MaoC_dehydratas; 1.
PIRSF; PIRSF005562; FAS_yeast_beta; 1.
PRINTS; PR01483; FASYNTHASE.
SMART; SM00827; PKS_AT; 1.
SUPFAM; SSF52151; SSF52151; 5.
SUPFAM; SSF54637; SSF54637; 2.
2: Evidence at transcript level;
Complete proteome; Hydrolase; Lyase; Multifunctional enzyme; NAD;
NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 1888 Fatty acid synthase beta subunit aflB.
/FTId=PRO_0000438337.
DOMAIN 1399 1500 MaoC-like. {ECO:0000255}.
REGION 23 395 Acetyltransferase (AT) domain.
{ECO:0000255,
ECO:0000305|PubMed:16256699}.
REGION 437 682 Enoyl reductase (ER) domain.
{ECO:0000255,
ECO:0000305|PubMed:16256699}.
REGION 990 1478 Dehydratase (DH) domain. {ECO:0000255,
ECO:0000305|PubMed:16256699}.
REGION 1517 1877 Malonyl/palmitoyl transferase (MT/PT)
domain. {ECO:0000255,
ECO:0000305|PubMed:16256699}.
SEQUENCE 1888 AA; 210430 MW; EC232BC88FA5F05C CRC64;
MGSVSREHES IPIQAAQRGA ARICAAFGGQ GSNNLDVLKG LLELYKRYGP DLDELLDVAS
NTLSQLASSP AAIDVHEPWG FDLRQWLTTP EVAPSKEILA LPPRSFPLNT LLSLALYCAT
CRELELDPGQ FRSLLHSSTG HSQGILAAVA ITQAESWPTF YDACRTVLQI SFWIGLEAYL
FTPSSAASDA MIQDCIEHGE GLLSSMLSVS GLSRSQVERV IEHVNKGLGE CNRWVHLALV
NSHEKFVLAG PPQSLWAVCL HVRRIRADND LDQSRILFRN RKPIVDILFL PISAPFHTPY
LDGVQDRVIE ALSSASLALH SIKIPLYHTG TGSNLQELQP HQLIPTLIRA ITVDQLDWPL
VCRGLNATHV LDFGPGQTCS LIQELTQGTG VSVIQLTTQS GPKPVGGHLA AVNWEAEFGL
RLHANVHGAA KLHNRMTTLL GKPPVMVAGM TPTTVRWDFV AAVAQAGYHV ELAGGGYHAE
RQFEAEIRRL ATAIPADHGI TCNLLYAKPT TFSWQISVIK DLVRQGVPVE GITIGAGIPS
PEVVQECVQS IGLKHISFKP GSFEAIHQVI QIARTHPNFL IGLQWTAGRG GGHHSWEDFH
GPILATYAQI RSCPNILLVV GSGFGGGPDT FPYLTGQWAQ AFGYPCMPFD GVLLGSRMMV
AREAHTSAQA KRLIIDAQGV GDADWHKSFD EPTGGVVTVN SEFGQPIHVL ATRGVMLWKE
LDNRVFSIKD TSKRLEYLRN HRQEIVSRLN ADFARPWFAV DGHGQNVELE DMTYLEVLRR
LCDLTYVSHQ KRWVDPSYRI LLLDFVHLLR ERFQCAIDNP GEYPLDIIVR VEESLKDKAY
RTLYPEDVSL LMHLFSRRDI KPVPFIPRLD ERFETWFKKD SLWQSEDVEA VIGQDVQRIF
IIQGPMAVQY SISDDESVKD ILHNICNHYV EALQADSRET SIGDVHSITQ KPLSAFPGLK
VTTNRVQGLY KFEKVGAVPE MDVLFEHIVG LSKSWARTCL MSKSVFRDGS RLHNPIRAAL
QLQRGDTIEV LLTADSEIRK IRLISPTGDG GSTSKVVLEI VSNDGQRVFA TLAPNIPLSP
EPSVVFCFKV DQKPNEWTLE EDASGRAERI KALYMSLWNL GFPNKASVLG LNSQFTGEEL
MITTDKIRDF ERVLRQTSPL QLQSWNPQGC VPIDYCVVIA WSALTKPLMV SSLKCDLLDL
LHSAISFHYA PSVKPLRVGD IVKTSSRILA VSVRPRGTML TVSADIQRQG QHVVTVKSDF
FLGGPVLACE TPFELTEEPE MVVHVDSEVR RAILHSRKWL MREDRALDLL GRQLLFRLKS
EKLFRPDGQL ALLQVTGSVF SYSPDGSTTA FGRVYFESES CTGNVVMDFL HRYGAPRAQL
LELQHPGWTG TSTVAVRGPR RSQSYARVSL DHNPIHVCPA FARYAGLSGP IVHGMETSAM
MRRIAEWAIG DADRSRFRSW HITLQAPVHP NDPLRVELQH KAMEDGEMVL KVQAFNERTE
ERVAEADAHV EQETTAYVFC GQGSQRQGMG MDLYVNCPEA KALWARADKH LWEKYGFSIL
HIVQNNPPAL TVHFGSQRGR RIRANYLRMM GQPPIDGRHP PILKGLTRNS TSYTFSYSQG
LLMSTQFAQP ALALMEMAQF EWLKAQGVVQ KGARFAGHSL GEYAALGACA SFLSFEDLIS
LIFYRGLKMQ NALPRDANGH TDYGMLAADP SRIGKGFEEA SLKCLVHIIQ QETGWFVEVV
NYNINSQQYV CAGHFRALWM LGKICDDLSC HPQPETVEGQ ELRAMVWKHV PTVEQVPRED
RMERGRATIP LPGIDIPYHS TMLRGEIEPY REYLSERIKV GDVKPCELVG RWIPNVVGQP
FSVDKSYVQL VHGITGSPRL HSLLQQMA


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EIAAB14290 [Acyl-carrier-protein] malonyltransferase,Homo sapiens,Human,Malonyl-CoA-acyl carrier protein transacylase, mitochondrial,MCAT,MCT,Mitochondrial malonyltransferase,MT
EIAAB14289 [Acyl-carrier-protein] malonyltransferase,Malonyl-CoA-acyl carrier protein transacylase, mitochondrial,Mcat,MCT,Mitochondrial malonyltransferase,Mouse,Mt,Mus musculus
EIAAB12849 3-keto acyl-CoA synthase ELOVL6,Elongation of very long chain fatty acids protein 6,ELOVL6,FACE,Fatty acid elongase 2,Fatty acyl-CoA elongase,hELO2,Homo sapiens,Human,LCE,Long-chain fatty-acyl elongas
EIAAB12846 3-keto acyl-CoA synthase Elovl6,Elongation of very long chain fatty acids protein 6,Elovl6,Face,Fatty acid elongase 2,Fatty acyl-CoA elongase,Lce,Long-chain fatty-acyl elongase,Rat,Rattus norvegicus,r
abx109426 Polyclonal Rabbit Enoyl-[acyl-carrier-protein] reductase [NADH] Antibody 100 μg
abx109170 Polyclonal Rabbit Enoyl-[acyl-carrier-protein] reductase [NADH] Antibody (HRP) 100 μg
EIAAB29419 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial,Beta-ketoacyl-ACP synthase,Bos taurus,Bovine,OXSM
EIAAB29421 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial,Beta-ketoacyl-ACP synthase,Mouse,Mus musculus,Oxsm
EIAAB12848 3-keto acyl-CoA synthase Elovl6,Elongation of very long chain fatty acids protein 6,Elovl6,Face,Fatty acyl-CoA elongase,Lce,Long chain fatty acid elongase,Masr,Mouse,Mus musculus,Myelin-associated SUR
EIAAB29420 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial,Beta-ketoacyl-ACP synthase,Homo sapiens,Human,OXSM
orb70386 Acyl Carrier Protein (65-74) peptide This is Acyl Carrier Protein (65-74) peptide. For research use only. 1 mg
orb70387 Acyl Carrier Protein (65-74) peptide This is Acyl Carrier Protein (65-74) peptide. For research use only. 1 mg
EIAAB37321 Mch,Olah,Oleoyl-ACP hydrolase,Rat,Rattus norvegicus,S-acyl fatty acid synthase thioesterase, medium chain,Thedc1,Thioesterase domain-containing protein 1,Thioesterase II
EIAAB37319 Mouse,Mus musculus,Olah,Oleoyl-ACP hydrolase,S-acyl fatty acid synthase thioesterase, medium chain,Thedc1,Thioesterase domain-containing protein 1,Thioesterase II
EIAAB36854 ACSVL3,FATP3,FATP-3,Fatty acid transport protein 3,Homo sapiens,Human,Long-chain fatty acid transport protein 3,PSEC0067,SLC27A3,Solute carrier family 27 member 3,UNQ367_PRO703,Very long-chain acyl-Co
E1560h Mouse ELISA Kit FOR 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial 96T
CSB-EL017313MO Mouse 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial(OXSM) ELISA kit 96T
CSB-EL017313HU Human 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial(OXSM) ELISA kit 96T
CSB-EL017313BO Bovine 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial(OXSM) ELISA kit 96T
SP-86553-5 Acyl Carrier Protein (65_74) (acid) 5 mg
SP-86553-5 Acyl Carrier Protein (65-74) (acid) [Val-Gln-Ala-Ala-Ile-Asp-Tyr-Ile-Asn-Gly (MW: 1063.18)] 5 mg
CSB-EL017313HU Human 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial(OXSM) ELISA kit SpeciesHuman 96T
CSB-EL017313BO Bovine 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial(OXSM) ELISA kit SpeciesBovine 96T
CSB-EL017313MO Mouse 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial(OXSM) ELISA kit SpeciesMouse 96T
A-0501 Acyl Carrier Protein (ACP) (65-74) (acid) 98 percent C47H74N12O16 CAS: 5mg


 

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