Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Manganese lipoxygenase (Mn-LO) (MnLOX) (EC 1.13.11.-) (EC 1.13.11.45) (Linoleate 11S-lipoxygenase) (Linoleate 13R-lipoxygenase) (Manganese 13R-lipoxygenase) (13R-MnLOX)

 MNLOX_GAEGA             Reviewed;         618 AA.
Q8X151;
01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
13-APR-2016, sequence version 2.
20-JUN-2018, entry version 71.
RecName: Full=Manganese lipoxygenase {ECO:0000303|PubMed:12047377};
Short=Mn-LO {ECO:0000303|PubMed:15629124};
Short=MnLOX {ECO:0000303|PubMed:12047377};
EC=1.13.11.- {ECO:0000269|PubMed:15629124};
EC=1.13.11.45 {ECO:0000269|PubMed:15629124};
AltName: Full=Linoleate 11S-lipoxygenase {ECO:0000305|PubMed:9582345};
AltName: Full=Linoleate 13R-lipoxygenase {ECO:0000305|PubMed:9582345};
AltName: Full=Manganese 13R-lipoxygenase {ECO:0000303|PubMed:23233731};
Short=13R-MnLOX {ECO:0000303|PubMed:23233731};
Flags: Precursor;
Gaeumannomyces graminis var. avenae (Oat take-all root rot fungus).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Magnaporthales; Magnaporthaceae;
Gaeumannomyces.
NCBI_TaxID=36778;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND
GLYCOSYLATION.
STRAIN=CBS 870.73;
PubMed=12047377; DOI=10.1046/j.1432-1033.2002.02936.x;
Hornsten L., Su C., Osbourn A.E., Hellman U., Oliw E.H.;
"Cloning of the manganese lipoxygenase gene reveals homology with the
lipoxygenase gene family.";
Eur. J. Biochem. 269:2690-2697(2002).
[2]
SEQUENCE REVISION TO 52 AND 158, AND MUTAGENESIS OF GLY-332; LEU-336
AND PHE-337.
PubMed=22822060; DOI=10.1074/jbc.M112.364331;
Wennman A., Jerneren F., Hamberg M., Oliw E.H.;
"Catalytic convergence of manganese and iron lipoxygenases by
replacement of a single amino acid.";
J. Biol. Chem. 287:31757-31765(2012).
[3]
SUBCELLULAR LOCATION.
PubMed=9582345; DOI=10.1074/jbc.273.21.13072;
Su C., Oliw E.H.;
"Manganese lipoxygenase. Purification and characterization.";
J. Biol. Chem. 273:13072-13079(1998).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
MUTAGENESIS OF HIS-290; HIS-294; HIS-478; HIS-479; ASN-482; GLN-483
AND VAL-618, AND GLYCOSYLATION.
PubMed=15629124; DOI=10.1016/j.abb.2004.10.026;
Cristea M., Engstroem K., Su C., Hoernsten L., Oliw E.H.;
"Expression of manganese lipoxygenase in Pichia pastoris and site-
directed mutagenesis of putative metal ligands.";
Arch. Biochem. Biophys. 434:201-211(2005).
[5]
MUTAGENESIS OF GLY-332.
PubMed=16641090; DOI=10.1074/jbc.M510311200;
Cristea M., Oliw E.H.;
"A G316A mutation of manganese lipoxygenase augments hydroperoxide
isomerase activity: mechanism of biosynthesis of epoxyalcohols.";
J. Biol. Chem. 281:17612-17623(2006).
[6]
MUTAGENESIS OF GLY-332; ASN-482 AND SER-485.
PubMed=18024999; DOI=10.1194/jlr.M700514-JLR200;
Oliw E.H.;
"Factors influencing the rearrangement of bis-allylic hydroperoxides
by manganese lipoxygenase.";
J. Lipid Res. 49:420-428(2008).
[7]
MUTAGENESIS OF PHE-347.
PubMed=23233731; DOI=10.1194/jlr.M033787;
Wennman A., Oliw E.H.;
"Secretion of two novel enzymes, manganese 9S-lipoxygenase and epoxy
alcohol synthase, by the rice pathogen Magnaporthe salvinii.";
J. Lipid Res. 54:762-775(2013).
-!- FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-
linolenic acids to 11S- and 13R-hydroperoxy fatty acids. At the
end of lipoxygenation, the intermediate product 11S-HPODE from
linoleic acid is then transformed into 13R-HPODE as the final
product. It also acts on alpha-linolenic acid producing 11S-HPOTrE
and 13R-HPOTrE with subsequent transformation of 11S-HPOTrE to
13R-HPOTrE as final product. {ECO:0000269|PubMed:15629124}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,12Z)-(11S)-11-
hydroperoxyoctadeca-9,12-dienoate. {ECO:0000269|PubMed:15629124}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,11E)-(13R)-13-
hydroperoxyoctadeca-9,11-dienoate. {ECO:0000269|PubMed:15629124}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (9Z,12Z,15Z)-(11S)-
11-hydroperoxyoctadeca-9,12,15-trienoate.
{ECO:0000269|PubMed:15629124}.
-!- CATALYTIC ACTIVITY: Alpha-linolenate + O(2) = (9Z,11E,15Z)-(13R)-
13-hydroperoxyoctadeca-9,11,15-trienoate.
{ECO:0000269|PubMed:15629124}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15629124};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.1 uM for alpha-linoleate {ECO:0000269|PubMed:15629124};
Vmax=18 nmol/min/ug enzyme for alpha-linoleate
{ECO:0000269|PubMed:15629124};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12047377,
ECO:0000269|PubMed:9582345}.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12047377,
ECO:0000269|PubMed:15629124}.
-!- SIMILARITY: Belongs to the lipoxygenase family. Manganese
lipoxygenase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY040824; AAK81882.2; -; Genomic_DNA.
PDB; 5FX8; X-ray; 2.60 A; A/B=1-618.
PDBsum; 5FX8; -.
ProteinModelPortal; Q8X151; -.
SMR; Q8X151; -.
SwissLipids; SLP:000001656; -.
KEGG; ag:AAK81882; -.
KO; K21794; -.
SABIO-RK; Q8X151; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0050584; F:linoleate 11-lipoxygenase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
InterPro; IPR000907; LipOase.
InterPro; IPR013819; LipOase_C.
InterPro; IPR036226; LipOase_C_sf.
PANTHER; PTHR11771; PTHR11771; 1.
Pfam; PF00305; Lipoxygenase; 1.
SUPFAM; SSF48484; SSF48484; 1.
PROSITE; PS51393; LIPOXYGENASE_3; 1.
1: Evidence at protein level;
3D-structure; Dioxygenase; Glycoprotein; Manganese; Metal-binding;
Oxidoreductase; Secreted; Signal.
SIGNAL 1 16 {ECO:0000250|UniProtKB:Q8X150}.
CHAIN 17 618 Manganese lipoxygenase.
/FTId=PRO_0000430459.
DOMAIN 47 618 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 290 290 Manganese; catalytic.
{ECO:0000305|PubMed:15629124}.
METAL 294 294 Manganese; catalytic.
{ECO:0000305|PubMed:15629124}.
METAL 478 478 Manganese; catalytic.
{ECO:0000305|PubMed:15629124}.
METAL 482 482 Manganese; catalytic.
{ECO:0000250|UniProtKB:G4NAP4}.
METAL 618 618 Manganese; catalytic; via carboxylate.
{ECO:0000305|PubMed:15629124}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 290 290 H->Q: Loses manganese cofactor and
abolishes catalytic activity.
{ECO:0000269|PubMed:15629124}.
MUTAGEN 294 294 H->E: Loses manganese cofactor and
abolishes catalytic activity.
{ECO:0000269|PubMed:15629124}.
MUTAGEN 332 332 G->A: Increases the hydroperoxide
isomerase activity severalfold and
chnages the regiospecificity of the
enzyme, slightly shifting the position of
oxygenation from the n-6 toward the n-8
and n-10 carbons. May do so by changing
the interaction of the hydroperoxides
with the catalytic metal.
{ECO:0000269|PubMed:16641090,
ECO:0000269|PubMed:18024999,
ECO:0000269|PubMed:22822060}.
MUTAGEN 332 332 G->V,S,T: Abolishes catalytic activity.
{ECO:0000269|PubMed:18024999}.
MUTAGEN 336 336 L->F: Increases the hydroperoxide
isomerase activity.
{ECO:0000269|PubMed:22822060}.
MUTAGEN 336 336 L->V,A,G: Changes the regiospecificity of
the enzyme from C-13 toward C-9 with
formation of 9S- and 9R-hydroperoxy fatty
acids. {ECO:0000269|PubMed:22822060}.
MUTAGEN 337 337 F->I: Changes the stereospecificity of
the enzyme from 100% 13R- to 69-74% 13S-
hydroperoxy fatty acids and increases the
oxygenation at C-9, producing mainly the
9S-hydroperoxy stereoisomer from linoleic
acid and the 9R-hydroperoxy stereoisomer
from alpha-linolenic acid.
{ECO:0000269|PubMed:22822060}.
MUTAGEN 337 337 F->V,A: Abolishes catalytic activity.
{ECO:0000269|PubMed:22822060}.
MUTAGEN 347 347 F->A: Changes the stereospecificity of
the enzyme from 13R-HPODE to 13R-, 9S-,
and 11-HPODE with almost complete
consumption of 11-HPODE to 13R- and 9S-
HPOTrE as end products from oxigenation
of linoleic acid. Does not affect
oxigenation of alpha-linolenic acid.
{ECO:0000269|PubMed:22822060}.
MUTAGEN 347 347 F->L,V: Changes the stereospecificity of
the enzyme from 13R-HPODE to 9S-HPODE as
end product from oxigenation of linoleic
acid and to 9S- and 13R-HPOTrE from
alpha-linolenic acid.
{ECO:0000269|PubMed:22822060}.
MUTAGEN 478 478 H->E: Loses manganese cofactor and
abolishes catalytic activity.
{ECO:0000269|PubMed:15629124}.
MUTAGEN 479 479 H->Q: No effect.
{ECO:0000269|PubMed:15629124}.
MUTAGEN 482 482 N->Q,L: No effect.
{ECO:0000269|PubMed:15629124,
ECO:0000269|PubMed:18024999}.
MUTAGEN 483 483 Q->N: No effect.
{ECO:0000269|PubMed:15629124}.
MUTAGEN 485 485 S->A: No effect.
{ECO:0000269|PubMed:18024999}.
MUTAGEN 618 618 Missing: Loses manganese cofactor and
abolishes catalytic activity.
{ECO:0000269|PubMed:15629124}.
HELIX 56 69 {ECO:0000244|PDB:5FX8}.
STRAND 70 73 {ECO:0000244|PDB:5FX8}.
STRAND 77 81 {ECO:0000244|PDB:5FX8}.
STRAND 83 85 {ECO:0000244|PDB:5FX8}.
HELIX 86 124 {ECO:0000244|PDB:5FX8}.
HELIX 131 137 {ECO:0000244|PDB:5FX8}.
TURN 138 140 {ECO:0000244|PDB:5FX8}.
TURN 143 145 {ECO:0000244|PDB:5FX8}.
TURN 152 159 {ECO:0000244|PDB:5FX8}.
HELIX 161 166 {ECO:0000244|PDB:5FX8}.
HELIX 167 169 {ECO:0000244|PDB:5FX8}.
TURN 181 183 {ECO:0000244|PDB:5FX8}.
HELIX 192 199 {ECO:0000244|PDB:5FX8}.
HELIX 203 208 {ECO:0000244|PDB:5FX8}.
STRAND 212 216 {ECO:0000244|PDB:5FX8}.
HELIX 218 222 {ECO:0000244|PDB:5FX8}.
STRAND 235 241 {ECO:0000244|PDB:5FX8}.
TURN 242 245 {ECO:0000244|PDB:5FX8}.
STRAND 246 253 {ECO:0000244|PDB:5FX8}.
HELIX 268 305 {ECO:0000244|PDB:5FX8}.
HELIX 313 321 {ECO:0000244|PDB:5FX8}.
TURN 322 324 {ECO:0000244|PDB:5FX8}.
HELIX 325 327 {ECO:0000244|PDB:5FX8}.
HELIX 328 335 {ECO:0000244|PDB:5FX8}.
HELIX 342 346 {ECO:0000244|PDB:5FX8}.
HELIX 351 363 {ECO:0000244|PDB:5FX8}.
HELIX 370 372 {ECO:0000244|PDB:5FX8}.
HELIX 374 380 {ECO:0000244|PDB:5FX8}.
STRAND 384 389 {ECO:0000244|PDB:5FX8}.
HELIX 396 420 {ECO:0000244|PDB:5FX8}.
HELIX 428 431 {ECO:0000244|PDB:5FX8}.
HELIX 434 444 {ECO:0000244|PDB:5FX8}.
TURN 445 447 {ECO:0000244|PDB:5FX8}.
HELIX 460 475 {ECO:0000244|PDB:5FX8}.
HELIX 477 481 {ECO:0000244|PDB:5FX8}.
HELIX 485 488 {ECO:0000244|PDB:5FX8}.
TURN 489 491 {ECO:0000244|PDB:5FX8}.
TURN 493 495 {ECO:0000244|PDB:5FX8}.
STRAND 498 500 {ECO:0000244|PDB:5FX8}.
STRAND 506 508 {ECO:0000244|PDB:5FX8}.
TURN 520 522 {ECO:0000244|PDB:5FX8}.
HELIX 526 539 {ECO:0000244|PDB:5FX8}.
TURN 542 548 {ECO:0000244|PDB:5FX8}.
HELIX 551 553 {ECO:0000244|PDB:5FX8}.
HELIX 558 563 {ECO:0000244|PDB:5FX8}.
HELIX 566 587 {ECO:0000244|PDB:5FX8}.
STRAND 600 602 {ECO:0000244|PDB:5FX8}.
TURN 609 611 {ECO:0000244|PDB:5FX8}.
STRAND 612 615 {ECO:0000244|PDB:5FX8}.
SEQUENCE 618 AA; 67583 MW; 466CFB2801B1D6F2 CRC64;
MRSRILAIVF AARHVAALPL AAEDAAATLS LTSSASSTTV LPSPTQYTLP NNDPNQGARN
ASIARKRELF LYGPSTLGQT TFYPTGELGN NISARDVLLW RQDAANQTAT AYREANETFA
DITSRGGFKT LDDFALLYNG HWKESVPEGI SKGMLSNCTS DLLFSMERLS SNPYVLKRLH
PTKDKLPFSV ESKVVKKLTA TTLEALHKGG RLFLVDHSYQ KKYTPQPGRY AAACQGLFYL
DARSNQFLPL AIKTNVGVDL TYTPLDDKDD WLLAKIMFNN NDLFYSQMYH VLFHTIPEIV
HEAAFRTLSD RHPVMGVLNR LMYQAYAIRP VGGAVLFNPG GFWDQNFGLP ASAAIDFPGS
VYAQGGGGFQ AGYLEKDLRS RGLIGEDSGP RLPHFPFYED AHRLIGAIRR FMQAFVDSTY
GADDGDDGAL LRDYELQNWI AEANGPAQVR DFPAAPLRRR AQLVDVLTHV AWITGGAHHV
MNQGSPVKFS GVLPLHPAAL YAPIPTAKGA TGNGTRAGLL AWLPNERQAV EQVSLLARFN
RAQVGDRKQT VRDAFAAPDL LAGNGPGYAA ANARFVEDTG RISREIAGRG FDGKGLSQGM
PFVWTALNPA VNPFFLSV


Related products :

Catalog number Product name Quantity
U1356m CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,8S-lipoxygenase,8S-LOX,Alox15b,Alox8,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Mouse,Mus musculus 96T
E1356m ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,8S-lipoxygenase,8S-LOX,Alox15b,Alox8,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Mouse,Mus musculus 96T
E1356m ELISA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,8S-lipoxygenase,8S-LOX,Alox15b,Alox8,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Mouse,Mus musculus 96T
U0891Rb CLIA 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
E0891Rb ELISA kit 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
E0891Rb ELISA 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
U1965h CLIA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
U1965h CLIA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
E1965h ELISA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
E1965h ELISA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
U1965m CLIA 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
U1965m CLIA kit 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
E1965m ELISA 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
E1965m ELISA kit 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
E1356h ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human 96T
U1356h CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human 96T
E1356h ELISA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human 96T
E1356r ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus 96T
E1356r ELISA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus 96T
U1356r CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus 96T
U1965b CLIA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
U1965b CLIA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
E1965b ELISA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
E1965b ELISA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
E1355r ELISA kit 5-lipoxygenase,5-LO,Alox5,Arachidonate 5-lipoxygenase,Rat,Rattus norvegicus 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur