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Bifunctional abietadiene synthase, chloroplastic ((-)-abieta-7(8),13(14)-diene synthase) (Abietadiene cyclase) (AgAS) (Agggabi) [Includes: Abietadiene synthase (EC 4.2.3.18) (Neoabietadiene synthase) (EC 4.2.3.132); Copalyl diphosphate synthase (EC 5.5.1.12)]

 TPSDV_ABIGR             Reviewed;         868 AA.
Q38710; Q94FW1;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-MAY-2017, entry version 93.
RecName: Full=Bifunctional abietadiene synthase, chloroplastic;
AltName: Full=(-)-abieta-7(8),13(14)-diene synthase;
AltName: Full=Abietadiene cyclase;
Short=AgAS;
AltName: Full=Agggabi;
Includes:
RecName: Full=Abietadiene synthase;
EC=4.2.3.18 {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
AltName: Full=Neoabietadiene synthase;
EC=4.2.3.132 {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
Includes:
RecName: Full=Copalyl diphosphate synthase;
EC=5.5.1.12 {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
Flags: Precursor;
Name=AS; Synonyms=ac22, ag22;
Abies grandis (Grand fir) (Pinus grandis).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Pinidae; Pinales; Pinaceae; Abies.
NCBI_TaxID=46611;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 148-166; 522-530;
615-625 AND 699-705, AND INDUCTION.
TISSUE=Stem;
PubMed=8798524; DOI=10.1074/jbc.271.38.23262;
Stoffer Vogel B., Wildung M.R., Vogel G., Croteau R.B.;
"Abietadiene synthase from grand fir (Abies grandis). cDNA isolation,
characterization, and bacterial expression of a bifunctional diterpene
cyclase involved in resin acid biosynthesis.";
J. Biol. Chem. 271:23262-23268(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-868, AND NOMENCLATURE.
PubMed=11404343;
Trapp S.C., Croteau R.B.;
"Genomic organization of plant terpene synthases and molecular
evolutionary implications.";
Genetics 158:811-832(2001).
[3]
GENE FAMILY, NOMENCLATURE, AND FUNCTION.
PubMed=9539701; DOI=10.1073/pnas.95.8.4126;
Bohlmann J., Meyer-Gauen G., Croteau R.B.;
"Plant terpenoid synthases: molecular biology and phylogenetic
analysis.";
Proc. Natl. Acad. Sci. U.S.A. 95:4126-4133(1998).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
ENZYME REGULATION.
PubMed=11112547; DOI=10.1021/bi001997l;
Peters R.J., Flory J.E., Jetter R., Ravn M.M., Lee H.J., Coates R.M.,
Croteau R.B.;
"Abietadiene synthase from grand fir (Abies grandis): characterization
and mechanism of action of the 'pseudomature' recombinant enzyme.";
Biochemistry 39:15592-15602(2000).
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10814381; DOI=10.1021/ol991230p;
Ravn M.M., Coates R.M., Flory J.E., Peters R.J., Croteau R.;
"Stereochemistry of the cyclization-rearrangement of (+)-copalyl
diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene
synthase from Abies grandis.";
Org. Lett. 2:573-576(2000).
[6]
MUTAGENESIS OF ASP-404 AND ASP-621, AND CHARACTERIZATION.
PubMed=11552804; DOI=10.1021/ja010670k;
Peters R.J., Ravn M.M., Coates R.M., Croteau R.B.;
"Bifunctional abietadiene synthase: free diffusive transfer of the
(+)-copalyl diphosphate intermediate between two distinct active
sites.";
J. Am. Chem. Soc. 123:8974-8978(2001).
[7]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, AND
MUTAGENESIS OF TRP-358; ASP-361; ARG-365; ASP-402; ASP-404; ASP-405;
ARG-411; ARG-454; GLU-499 AND TYR-520.
PubMed=11827528; DOI=10.1021/bi011879d;
Peters R.J., Croteau R.B.;
"Abietadiene synthase catalysis: conserved residues involved in
protonation-initiated cyclization of geranylgeranyl diphosphate to
(+)-copalyl diphosphate.";
Biochemistry 41:1836-1842(2002).
[8]
MUTAGENESIS OF ARG-584; ARG-586; GLU-589; THR-617; ASP-621; ASP-625;
GLU-699; SER-721; ARG-762; ASN-765; ASP-766; THR-769; GLU-773;
GLU-778; TYR-841; ASP-845 AND THR-848, AND CHARACTERIZATION.
PubMed=11805316; DOI=10.1073/pnas.022627099;
Peters R.J., Croteau R.B.;
"Abietadiene synthase catalysis: mutational analysis of a prenyl
diphosphate ionization-initiated cyclization and rearrangement.";
Proc. Natl. Acad. Sci. U.S.A. 99:580-584(2002).
[9]
FUNCTION, AND MUTAGENESIS OF LYS-86 AND ARG-87.
PubMed=12614165; DOI=10.1021/bi020492n;
Peters R.J., Carter O.A., Zhang Y., Matthews B.W., Croteau R.B.;
"Bifunctional abietadiene synthase: mutual structural dependence of
the active sites for protonation-initiated and ionization-initiated
cyclizations.";
Biochemistry 42:2700-2707(2003).
[10]
FUNCTION, AND MUTAGENESIS OF ALA-723.
PubMed=18052062; DOI=10.1021/ja074977g;
Wilderman P.R., Peters R.J.;
"A single residue switch converts abietadiene synthase into a
pimaradiene specific cyclase.";
J. Am. Chem. Soc. 129:15736-15737(2007).
[11]
FUNCTION, AND MUTAGENESIS OF ARG-356 AND ASP-621.
PubMed=20430888; DOI=10.1074/jbc.M110.123307;
Mann F.M., Prisic S., Davenport E.K., Determan M.K., Coates R.M.,
Peters R.J.;
"A single residue switch for Mg(2+)-dependent inhibition characterizes
plant class II diterpene cyclases from primary and secondary
metabolism.";
J. Biol. Chem. 285:20558-20563(2010).
[12]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 85-868, AND MUTAGENESIS OF
ASN-451 AND VAL-727.
PubMed=22219188; DOI=10.1074/jbc.M111.337592;
Zhou K., Gao Y., Hoy J.A., Mann F.M., Honzatko R.B., Peters R.J.;
"Insights into diterpene cyclization from structure of bifunctional
abietadiene synthase from Abies grandis.";
J. Biol. Chem. 287:6840-6850(2012).
-!- FUNCTION: Involved in defensive oleoresin formation in conifers in
response to insect attack or other injury. Involved in diterpene
(C20) olefins biosynthesis. Bifunctional enzyme that catalyzes two
sequential cyclizations of geranylgeranyl diphosphate (GGPP) to
abietadiene. The copalyl diphosphate (CPP) intermediate diffuses
freely between the 2 active sites in the enzyme. Changes in
reaction pH, but not salt concentration, influence the relative
proportion of the major products of the enzyme, abitadiene,
levopimaradiene and neoabitadiene. {ECO:0000269|PubMed:10814381,
ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528,
ECO:0000269|PubMed:12614165, ECO:0000269|PubMed:18052062,
ECO:0000269|PubMed:20430888, ECO:0000269|PubMed:9539701}.
-!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate = (+)-copalyl
diphosphate. {ECO:0000269|PubMed:10814381,
ECO:0000269|PubMed:11112547}.
-!- CATALYTIC ACTIVITY: (+)-copalyl diphosphate = abieta-7,13-diene +
diphosphate. {ECO:0000269|PubMed:10814381,
ECO:0000269|PubMed:11112547}.
-!- CATALYTIC ACTIVITY: (+)-copalyl diphosphate = neoabietadiene +
diphosphate. {ECO:0000269|PubMed:10814381,
ECO:0000269|PubMed:11112547}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q40577};
Note=Binds 3 Mg(2+) ions per subunit.
{ECO:0000250|UniProtKB:Q40577};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
-!- ENZYME REGULATION: Not inhibited by 13-cyclopropylidene or 16-
methylidenegeranylgeranyl diphosphate. The copalyl diphosphate
synthase activity is not susceptible to magnesium-dependent
inhibition. {ECO:0000269|PubMed:11112547}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3 uM for GGPP (in presence of magnesium)
{ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
KM=20 uM for GGPP (in absence of magnesium)
{ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
KM=0.4 uM for CPP (in presence of magnesium)
{ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
KM=10 uM for CPP (in absence of magnesium)
{ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
pH dependence:
Optimum pH is 7.2 with GGPP as substrate and 8.7 with CPP as
substrate. {ECO:0000269|PubMed:11112547,
ECO:0000269|PubMed:11827528};
-!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
-!- INDUCTION: By wounding. {ECO:0000269|PubMed:8798524}.
-!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the
catalytic activity in the class II active site relevant for the
cyclization of GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif
is important for the catalytic activity in the class I active
site, presumably through binding to Mg(2+). {ECO:0000305}.
-!- PTM: The N-terminus is blocked.
-!- MISCELLANEOUS: The abietadiene synthase activity exhibits an
absolute dependence on a divalent metal ion cofactor while the
copalyl diphosphate synthase activity is not completely dependent.
-!- SIMILARITY: Belongs to the terpene synthase family. Tpsd
subfamily. {ECO:0000305}.
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EMBL; U50768; AAB05407.1; -; mRNA.
EMBL; AF326516; AAK83563.1; -; Genomic_DNA.
PDB; 3S9V; X-ray; 2.30 A; A/B/C/D=85-868.
PDBsum; 3S9V; -.
ProteinModelPortal; Q38710; -.
SMR; Q38710; -.
PRIDE; Q38710; -.
KEGG; ag:AAB05407; -.
KO; K12927; -.
BioCyc; MetaCyc:MONOMER-12822; -.
BRENDA; 4.2.3.132; 2.
BRENDA; 4.2.3.18; 2.
UniPathway; UPA00924; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0050554; F:abietadiene synthase activity; IEA:UniProtKB-EC.
GO; GO:0050559; F:copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
Gene3D; 1.10.600.10; -; 1.
Gene3D; 1.50.10.130; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom.
InterPro; IPR001906; Terpene_synth_N.
InterPro; IPR005630; Terpene_synthase_metal-bd.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF01397; Terpene_synth; 1.
Pfam; PF03936; Terpene_synth_C; 1.
SUPFAM; SSF48239; SSF48239; 3.
SUPFAM; SSF48576; SSF48576; 1.
1: Evidence at protein level;
3D-structure; Chloroplast; Direct protein sequencing; Isomerase;
Lyase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
Plastid; Transit peptide.
TRANSIT 1 70 Chloroplast. {ECO:0000255}.
CHAIN 71 868 Bifunctional abietadiene synthase,
chloroplastic.
/FTId=PRO_0000033634.
MOTIF 402 405 DXDD motif. {ECO:0000305}.
MOTIF 621 625 DDXXD motif. {ECO:0000305}.
METAL 621 621 Magnesium 1.
{ECO:0000250|UniProtKB:Q40577}.
METAL 621 621 Magnesium 2.
{ECO:0000250|UniProtKB:Q40577}.
METAL 625 625 Magnesium 1.
{ECO:0000250|UniProtKB:Q40577}.
METAL 625 625 Magnesium 2.
{ECO:0000250|UniProtKB:Q40577}.
METAL 765 765 Magnesium 3.
{ECO:0000250|UniProtKB:Q40577}.
METAL 769 769 Magnesium 3.
{ECO:0000250|UniProtKB:Q40577}.
METAL 773 773 Magnesium 3.
{ECO:0000250|UniProtKB:Q40577}.
MUTAGEN 86 86 K->A: No effect on CPP binding, but
decreased abietadiene synthase activity;
when associated with A-87.
{ECO:0000269|PubMed:12614165}.
MUTAGEN 87 87 R->A: No effect on CPP binding, but
decreased abietadiene synthase activity;
when associated with A-86.
{ECO:0000269|PubMed:12614165}.
MUTAGEN 356 356 R->A: No effect on abietadiene synthase
activity, but strongly reduced copalyl
diphosphate synthase activity.
{ECO:0000269|PubMed:20430888}.
MUTAGEN 356 356 R->H: Increased Mg(2+) inhibition; when
associated with A-621.
{ECO:0000269|PubMed:20430888}.
MUTAGEN 358 358 W->A: Decreased copalyl diphosphate
synthase activity.
{ECO:0000269|PubMed:11827528}.
MUTAGEN 361 361 D->A: No effect on GGPP binding, but
decreased copalyl diphosphate synthase
activity. {ECO:0000269|PubMed:11827528}.
MUTAGEN 365 365 R->A: No effect on GGPP binding, but
decreased copalyl diphosphate synthase
activity. {ECO:0000269|PubMed:11827528}.
MUTAGEN 402 402 D->A,E,N: No effect on GGPP binding, but
decreased copalyl diphosphate synthase
activity. {ECO:0000269|PubMed:11827528}.
MUTAGEN 404 404 D->A,E,N: No effect on GGPP binding, but
loss of copalyl diphosphate synthase
activity. {ECO:0000269|PubMed:11552804,
ECO:0000269|PubMed:11827528}.
MUTAGEN 405 405 D->A,E,N: No effect on GGPP binding, but
decreased copalyl diphosphate synthase
activity. {ECO:0000269|PubMed:11827528}.
MUTAGEN 411 411 R->A: No effect on GGPP binding, but
slightly decreased copalyl diphosphate
synthase activity.
{ECO:0000269|PubMed:11827528}.
MUTAGEN 451 451 N->A: No effect on abietadiene synthase
activity, but strongly reduced copalyl
diphosphate synthase activity.
{ECO:0000269|PubMed:22219188}.
MUTAGEN 454 454 R->A: No effect on GGPP binding, but
decreased copalyl diphosphate synthase
activity. {ECO:0000269|PubMed:11827528}.
MUTAGEN 499 499 E->A: No effect on GGPP binding, but
decreased copalyl diphosphate synthase
activity. {ECO:0000269|PubMed:11827528}.
MUTAGEN 520 520 Y->A: No effect on GGPP binding, but
slightly decreased copalyl diphosphate
synthase activity.
{ECO:0000269|PubMed:11827528}.
MUTAGEN 584 584 R->A: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 586 586 R->A: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 589 589 E->A: Lower substrate binding and strong
decrease of abietadiene synthase
activity. {ECO:0000269|PubMed:11805316}.
MUTAGEN 617 617 T->A: Increased production of abietadiene
at the expense of levopimaradiene.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 621 621 D->A: Loss of abietadiene synthase
activity. Increased Mg(2+) inhibition;
when associated with H-356.
{ECO:0000269|PubMed:11552804,
ECO:0000269|PubMed:11805316,
ECO:0000269|PubMed:20430888}.
MUTAGEN 625 625 D->A: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 699 699 E->A: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 721 721 S->A: Lower substrate binding and strong
decrease of abietadiene synthase
activity. {ECO:0000269|PubMed:11805316}.
MUTAGEN 723 723 A->S: Produces pimaradienes instead of
abietadienes.
{ECO:0000269|PubMed:18052062}.
MUTAGEN 727 727 V->T: No effect.
{ECO:0000269|PubMed:22219188}.
MUTAGEN 762 762 R->A: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 765 765 N->A: Abolishes the conversion of CPP to
abietadiene; produces only
sandaracopimaradiene.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 766 766 D->A: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 769 769 T->A: Increased production of
neoabietadiene at the expense of both
levopimaradiene and abietadiene.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 773 773 E->A: Increased production of
neoabietadiene.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 778 778 E->A: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 841 841 Y->F: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 845 845 D->A: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
MUTAGEN 848 848 T->A: No or small effect on substrate
binding, but strongly decreases
abietadiene synthase activity.
{ECO:0000269|PubMed:11805316}.
CONFLICT 23 23 A -> T (in Ref. 2; AAK83563).
{ECO:0000305}.
CONFLICT 214 214 F -> S (in Ref. 2; AAK83563).
{ECO:0000305}.
CONFLICT 297 299 DWQ -> EWE (in Ref. 2; AAK83563).
{ECO:0000305}.
CONFLICT 557 557 V -> L (in Ref. 2; AAK83563).
{ECO:0000305}.
CONFLICT 579 579 D -> E (in Ref. 2; AAK83563).
{ECO:0000305}.
CONFLICT 653 653 Q -> K (in Ref. 2; AAK83563).
{ECO:0000305}.
HELIX 112 129 {ECO:0000244|PDB:3S9V}.
HELIX 139 145 {ECO:0000244|PDB:3S9V}.
STRAND 155 159 {ECO:0000244|PDB:3S9V}.
HELIX 160 168 {ECO:0000244|PDB:3S9V}.
STRAND 179 181 {ECO:0000244|PDB:3S9V}.
HELIX 184 200 {ECO:0000244|PDB:3S9V}.
HELIX 205 219 {ECO:0000244|PDB:3S9V}.
HELIX 220 224 {ECO:0000244|PDB:3S9V}.
HELIX 234 247 {ECO:0000244|PDB:3S9V}.
HELIX 257 270 {ECO:0000244|PDB:3S9V}.
HELIX 275 280 {ECO:0000244|PDB:3S9V}.
HELIX 284 291 {ECO:0000244|PDB:3S9V}.
TURN 293 295 {ECO:0000244|PDB:3S9V}.
HELIX 298 302 {ECO:0000244|PDB:3S9V}.
HELIX 315 325 {ECO:0000244|PDB:3S9V}.
HELIX 328 341 {ECO:0000244|PDB:3S9V}.
HELIX 352 365 {ECO:0000244|PDB:3S9V}.
HELIX 369 372 {ECO:0000244|PDB:3S9V}.
HELIX 373 384 {ECO:0000244|PDB:3S9V}.
HELIX 403 415 {ECO:0000244|PDB:3S9V}.
HELIX 422 428 {ECO:0000244|PDB:3S9V}.
HELIX 446 456 {ECO:0000244|PDB:3S9V}.
HELIX 464 480 {ECO:0000244|PDB:3S9V}.
TURN 481 483 {ECO:0000244|PDB:3S9V}.
STRAND 492 494 {ECO:0000244|PDB:3S9V}.
HELIX 496 505 {ECO:0000244|PDB:3S9V}.
HELIX 508 510 {ECO:0000244|PDB:3S9V}.
HELIX 513 523 {ECO:0000244|PDB:3S9V}.
STRAND 530 536 {ECO:0000244|PDB:3S9V}.
TURN 539 541 {ECO:0000244|PDB:3S9V}.
HELIX 544 574 {ECO:0000244|PDB:3S9V}.
TURN 575 578 {ECO:0000244|PDB:3S9V}.
STRAND 581 583 {ECO:0000244|PDB:3S9V}.
HELIX 587 597 {ECO:0000244|PDB:3S9V}.
HELIX 601 603 {ECO:0000244|PDB:3S9V}.
HELIX 604 624 {ECO:0000244|PDB:3S9V}.
HELIX 630 642 {ECO:0000244|PDB:3S9V}.
STRAND 644 647 {ECO:0000244|PDB:3S9V}.
HELIX 648 650 {ECO:0000244|PDB:3S9V}.
HELIX 653 677 {ECO:0000244|PDB:3S9V}.
HELIX 682 704 {ECO:0000244|PDB:3S9V}.
HELIX 711 721 {ECO:0000244|PDB:3S9V}.
HELIX 724 731 {ECO:0000244|PDB:3S9V}.
STRAND 735 737 {ECO:0000244|PDB:3S9V}.
HELIX 741 744 {ECO:0000244|PDB:3S9V}.
TURN 745 747 {ECO:0000244|PDB:3S9V}.
HELIX 752 776 {ECO:0000244|PDB:3S9V}.
HELIX 782 789 {ECO:0000244|PDB:3S9V}.
HELIX 795 819 {ECO:0000244|PDB:3S9V}.
HELIX 824 840 {ECO:0000244|PDB:3S9V}.
HELIX 851 863 {ECO:0000244|PDB:3S9V}.
SEQUENCE 868 AA; 99536 MW; AD5E79F56B70D25C CRC64;
MAMPSSSLSS QIPTAAHHLT ANAQSIPHFS TTLNAGSSAS KRRSLYLRWG KGSNKIIACV
GEGGATSVPY QSAEKNDSLS SSTLVKREFP PGFWKDDLID SLTSSHKVAA SDEKRIETLI
SEIKNMFRCM GYGETNPSAY DTAWVARIPA VDGSDNPHFP ETVEWILQNQ LKDGSWGEGF
YFLAYDRILA TLACIITLTL WRTGETQVQK GIEFFRTQAG KMEDEADSHR PSGFEIVFPA
MLKEAKILGL DLPYDLPFLK QIIEKREAKL KRIPTDVLYA LPTTLLYSLE GLQEIVDWQK
IMKLQSKDGS FLSSPASTAA VFMRTGNKKC LDFLNFVLKK FGNHVPCHYP LDLFERLWAV
DTVERLGIDR HFKEEIKEAL DYVYSHWDER GIGWARENPV PDIDDTAMGL RILRLHGYNV
SSDVLKTFRD ENGEFFCFLG QTQRGVTDML NVNRCSHVSF PGETIMEEAK LCTERYLRNA
LENVDAFDKW AFKKNIRGEV EYALKYPWHK SMPRLEARSY IENYGPDDVW LGKTVYMMPY
ISNEKYLELA KLDFNKVQSI HQTELQDLRR WWKSSGFTDL NFTRERVTEI YFSPASFIFE
PEFSKCREVY TKTSNFTVIL DDLYDAHGSL DDLKLFTESV KRWDLSLVDQ MPQQMKICFV
GFYNTFNDIA KEGRERQGRD VLGYIQNVWK VQLEAYTKEA EWSEAKYVPS FNEYIENASV
SIALGTVVLI SALFTGEVLT DEVLSKIDRE SRFLQLMGLT GRLVNDTKTY QAERGQGEVA
SAIQCYMKDH PKISEEEALQ HVYSVMENAL EELNREFVNN KIPDIYKRLV FETARIMQLF
YMQGDGLTLS HDMEIKEHVK NCLFQPVA


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Catalog number Product name Quantity
EIAAB11864 All-trans-decaprenyl-diphosphate synthase subunit 1,Decaprenyl pyrophosphate synthase subunit 1,Decaprenyl-diphosphate synthase subunit 1,Dps1,Mouse,Mus musculus,Pdss1,Solanesyl-diphosphate synthase s
EIAAB11424 All-trans-decaprenyl-diphosphate synthase subunit 2,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,Dlp1,Mouse,Mus musculus,Pdss2,Solanesyl-diphosphate synthase s
EIAAB06601 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,Homo sapiens,Human
EIAAB06603 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,Cds2,CTP phosphatidate cytidylyltransferase 2,Mouse,Mus musculus
EIAAB06597 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,CDS,CDS 1,CDS1,CTP phosphatidate cytidylyltransferase 1,Homo sapiens,H
EIAAB06599 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,Cds,CDS 1,Cds1,CTP phosphatidate cytidylyltransferase 1,Mouse,Mus musc
EIAAB06600 Bos taurus,Bovine,CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,
E0167h ELISA kit Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostag 96T
E0167h ELISA Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandi 96T
EIAAB28570 (2-5')oligo(A) synthase 1B,2-5A synthase 1B,2'-5'-oligoadenylate synthase 1B,2'-5'-oligoadenylate synthase-like protein 1,Mouse,Mus musculus,Oas1b,Oias2
E0167r ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
E0167b ELISA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167m ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167b ELISA kit Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
U0167b CLIA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167m ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
U0167r CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
U0167m CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167r ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
U0167p CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T
E0167p ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T
E0167p ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T
U0167h CLIA Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin 96T
E0122Rb ELISA COX1,COX-1,Cyclooxygenase-1,Oryctolagus cuniculus,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1,Rabbit 96T
E0699Rb ELISA COX2,COX-2,COX-2,Cyclooxygenase-2,Oryctolagus cuniculus,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2,Rabbit 96T


 

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