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

Asp/Glu-specific dipeptidyl-peptidase (EC 3.4.14.-) (Dipeptidyl-peptidase 11) (DPP11)

 DPP11_PORG3             Reviewed;         720 AA.
B2RID1;
17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 1.
23-MAY-2018, entry version 56.
RecName: Full=Asp/Glu-specific dipeptidyl-peptidase {ECO:0000303|PubMed:21896480};
EC=3.4.14.- {ECO:0000269|PubMed:21896480, ECO:0000269|PubMed:23246913};
AltName: Full=Dipeptidyl-peptidase 11 {ECO:0000303|PubMed:21896480};
Short=DPP11 {ECO:0000303|PubMed:21896480};
Flags: Precursor;
Name=dpp11 {ECO:0000312|EMBL:BAG33126.1};
OrderedLocusNames=PGN_0607 {ECO:0000312|EMBL:BAG33126.1};
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 /
JCM 12257 / NCTC 11834 / 2561).
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
Porphyromonadaceae; Porphyromonas.
NCBI_TaxID=431947;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
MUTAGENESIS OF SER-655.
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561;
PubMed=21896480; DOI=10.1074/jbc.M111.278572;
Ohara-Nemoto Y., Shimoyama Y., Kimura S., Kon A., Haraga H., Ono T.,
Nemoto T.K.;
"Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas
gingivalis ensures utilization of proteinaceous energy sources.";
J. Biol. Chem. 286:38115-38127(2011).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561;
PubMed=18524787; DOI=10.1093/dnares/dsn013;
Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
Nakayama K.;
"Determination of the genome sequence of Porphyromonas gingivalis
strain ATCC 33277 and genomic comparison with strain W83 revealed
extensive genome rearrangements in P. gingivalis.";
DNA Res. 15:215-225(2008).
[3]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND MUTAGENESIS
OF ARG-673.
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561;
PubMed=23246913; DOI=10.1016/j.biochi.2012.11.019;
Rouf S.M., Ohara-Nemoto Y., Hoshino T., Fujiwara T., Ono T.,
Nemoto T.K.;
"Discrimination based on Gly and Arg/Ser at position 673 between
dipeptidyl-peptidase (DPP) 7 and DPP11, widely distributed DPPs in
pathogenic and environmental gram-negative bacteria.";
Biochimie 95:824-832(2013).
[4]
X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS), DISULFIDE BOND, SUBUNIT, AND
MUTAGENESIS OF ARG-337 AND ARG-673.
PubMed=26057589; DOI=10.1038/srep11151;
Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S.,
Fujimoto M., Inaka K., Tanaka H., Yamada M., Ohta K., Gouda H.,
Nonaka T., Ogasawara W., Tanaka N.;
"Structural and mutational analyses of dipeptidyl peptidase 11 from
Porphyromonas gingivalis reveal the molecular basis for strict
substrate specificity.";
Sci. Rep. 5:11151-11151(2015).
-!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus
of oligopeptides. Shows a strict specificity for acidic residues
(Asp or Glu) in the P1 position, and has a hydrophobic residue
preference at the P2 position. Preferentially cleaves the
synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA)
as compared to Leu-Glu-MCA. Is involved in amino acid metabolism
and bacterial growth of asaccharolytic P.gingivalis, that utilizes
amino acids from extracellular proteinaceous nutrients as energy
and carbon sources. {ECO:0000269|PubMed:21896480,
ECO:0000269|PubMed:23246913}.
-!- ENZYME REGULATION: Enzyme activity is completely blocked by
diisopropyl-fluorophosphates, moderately by phenylmethylsulfonyl
fluoride (PMSF) and 4-(2-methyl)benzenesulfonyl fluoride, and
slightly by pepstatin in vitro. {ECO:0000269|PubMed:21896480}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.0. {ECO:0000269|PubMed:21896480};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26057589}.
-!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:21896480}.
Note=Is exclusively cell-associated.
{ECO:0000269|PubMed:21896480}.
-!- DISRUPTION PHENOTYPE: Cell growth is retarded. Complete loss of
hydrolysis for ac-DNLD- and LE-MCA. The efficiency of peptide
utilization of proteinaceous nutrients is reduced in mutant cells.
{ECO:0000269|PubMed:21896480}.
-!- SIMILARITY: Belongs to the peptidase S46 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; BR000944; FAA00730.1; -; Genomic_DNA.
EMBL; AP009380; BAG33126.1; -; Genomic_DNA.
RefSeq; WP_012457641.1; NZ_CP025930.1.
PDB; 4XZY; X-ray; 2.70 A; A/B=1-720.
PDB; 4Y01; X-ray; 2.46 A; A/B=1-720.
PDB; 4Y02; X-ray; 1.96 A; A=1-720.
PDB; 4Y04; X-ray; 1.66 A; A=1-720.
PDB; 5JWF; X-ray; 2.40 A; A/B=22-720.
PDBsum; 4XZY; -.
PDBsum; 4Y01; -.
PDBsum; 4Y02; -.
PDBsum; 4Y04; -.
PDBsum; 5JWF; -.
ProteinModelPortal; B2RID1; -.
SMR; B2RID1; -.
STRING; 431947.PGN_0607; -.
MEROPS; S46.002; -.
EnsemblBacteria; BAG33126; BAG33126; PGN_0607.
GeneID; 29255834; -.
KEGG; pgn:PGN_0607; -.
eggNOG; ENOG4105CZH; Bacteria.
eggNOG; ENOG410XPBV; LUCA.
HOGENOM; HOG000287550; -.
OMA; LFRIYAD; -.
BioCyc; PGIN431947:G1G2V-668-MONOMER; -.
Proteomes; UP000008842; Chromosome.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
GO; GO:0042277; F:peptide binding; IDA:UniProtKB.
GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:InterPro.
GO; GO:0048588; P:developmental cell growth; IMP:UniProtKB.
GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
InterPro; IPR019500; Pep_S46.
InterPro; IPR009003; Peptidase_S1_PA.
PANTHER; PTHR38469; PTHR38469; 1.
Pfam; PF10459; Peptidase_S46; 1.
SUPFAM; SSF50494; SSF50494; 3.
1: Evidence at protein level;
3D-structure; Aminopeptidase; Complete proteome; Disulfide bond;
Hydrolase; Protease; Serine protease; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 720 Asp/Glu-specific dipeptidyl-peptidase.
/FTId=PRO_5005662231.
ACT_SITE 85 85 Charge relay system.
{ECO:0000250|UniProtKB:V5YM14,
ECO:0000305|PubMed:26057589}.
ACT_SITE 227 227 Charge relay system.
{ECO:0000250|UniProtKB:V5YM14,
ECO:0000305|PubMed:26057589}.
ACT_SITE 655 655 Charge relay system.
{ECO:0000250|UniProtKB:V5YM14,
ECO:0000305|PubMed:21896480,
ECO:0000305|PubMed:26057589}.
SITE 673 673 Is essential for the Asp/Glu P1
specificity of DPP11; involved in the
recognition of the Asp/Glu residue at the
P1 position of substrate peptides.
{ECO:0000269|PubMed:26057589}.
DISULFID 69 86 {ECO:0000244|PDB:4XZY,
ECO:0000244|PDB:4Y02,
ECO:0000244|PDB:4Y04,
ECO:0000269|PubMed:26057589}.
MUTAGEN 337 337 R->A,N: Significant increase (or
preservation) of the catalytic activity.
{ECO:0000269|PubMed:26057589}.
MUTAGEN 655 655 S->A: Loss of catalytic activity.
{ECO:0000269|PubMed:21896480}.
MUTAGEN 673 673 R->A: Loss of catalytic activity.
{ECO:0000269|PubMed:26057589}.
MUTAGEN 673 673 R->G: Drastically decreased but still
significant activities against Asp/Glu
substrates, as well as detectable
activity against substrates harboring
hydrophobic residues at the P1 position.
{ECO:0000269|PubMed:26057589}.
MUTAGEN 673 673 R->S: The Asp/Glu preference is inverted,
i.e., peptidase activity toward Leu-Asp-
MCA nearly disappears, whereas that to
Leu-Glu-MCA partially remains.
{ECO:0000269|PubMed:23246913}.
HELIX 28 30 {ECO:0000244|PDB:4Y04}.
HELIX 31 40 {ECO:0000244|PDB:4Y04}.
HELIX 47 50 {ECO:0000244|PDB:4Y04}.
STRAND 53 55 {ECO:0000244|PDB:4Y04}.
HELIX 58 61 {ECO:0000244|PDB:4Y04}.
STRAND 62 65 {ECO:0000244|PDB:4Y04}.
TURN 66 68 {ECO:0000244|PDB:4Y04}.
STRAND 69 73 {ECO:0000244|PDB:4Y04}.
STRAND 79 82 {ECO:0000244|PDB:4Y04}.
HELIX 84 94 {ECO:0000244|PDB:4Y04}.
STRAND 97 99 {ECO:0000244|PDB:4Y02}.
HELIX 101 104 {ECO:0000244|PDB:4Y04}.
HELIX 111 113 {ECO:0000244|PDB:4Y04}.
STRAND 122 130 {ECO:0000244|PDB:4Y04}.
HELIX 132 139 {ECO:0000244|PDB:4Y04}.
HELIX 149 151 {ECO:0000244|PDB:4Y04}.
HELIX 153 164 {ECO:0000244|PDB:4Y04}.
TURN 166 171 {ECO:0000244|PDB:4Y04}.
STRAND 175 182 {ECO:0000244|PDB:4Y04}.
TURN 183 186 {ECO:0000244|PDB:4Y04}.
STRAND 187 196 {ECO:0000244|PDB:4Y04}.
STRAND 198 204 {ECO:0000244|PDB:4Y04}.
HELIX 207 210 {ECO:0000244|PDB:4Y04}.
TURN 211 219 {ECO:0000244|PDB:4Y04}.
STRAND 229 235 {ECO:0000244|PDB:4Y04}.
STRAND 259 262 {ECO:0000244|PDB:4Y02}.
STRAND 269 274 {ECO:0000244|PDB:4Y04}.
HELIX 285 293 {ECO:0000244|PDB:4Y04}.
HELIX 295 316 {ECO:0000244|PDB:4Y04}.
HELIX 318 347 {ECO:0000244|PDB:4Y04}.
HELIX 350 368 {ECO:0000244|PDB:4Y04}.
HELIX 372 400 {ECO:0000244|PDB:4Y04}.
TURN 401 404 {ECO:0000244|PDB:4Y04}.
HELIX 406 409 {ECO:0000244|PDB:4Y04}.
HELIX 415 421 {ECO:0000244|PDB:5JWF}.
STRAND 422 424 {ECO:0000244|PDB:4Y01}.
HELIX 431 443 {ECO:0000244|PDB:4Y04}.
HELIX 450 467 {ECO:0000244|PDB:4Y04}.
HELIX 470 472 {ECO:0000244|PDB:4Y04}.
HELIX 475 478 {ECO:0000244|PDB:4Y04}.
HELIX 479 482 {ECO:0000244|PDB:4Y04}.
TURN 483 486 {ECO:0000244|PDB:4Y04}.
HELIX 488 498 {ECO:0000244|PDB:4Y04}.
HELIX 504 510 {ECO:0000244|PDB:4Y04}.
TURN 516 521 {ECO:0000244|PDB:4Y04}.
HELIX 523 542 {ECO:0000244|PDB:4Y04}.
HELIX 543 545 {ECO:0000244|PDB:4Y04}.
HELIX 546 564 {ECO:0000244|PDB:4Y04}.
STRAND 566 568 {ECO:0000244|PDB:5JWF}.
STRAND 574 576 {ECO:0000244|PDB:4XZY}.
STRAND 578 584 {ECO:0000244|PDB:4Y04}.
STRAND 587 590 {ECO:0000244|PDB:4Y04}.
STRAND 593 595 {ECO:0000244|PDB:4Y04}.
STRAND 597 600 {ECO:0000244|PDB:4Y04}.
HELIX 601 607 {ECO:0000244|PDB:4Y04}.
HELIX 613 615 {ECO:0000244|PDB:4Y04}.
HELIX 619 627 {ECO:0000244|PDB:4Y04}.
HELIX 631 633 {ECO:0000244|PDB:4Y01}.
STRAND 636 638 {ECO:0000244|PDB:5JWF}.
STRAND 641 646 {ECO:0000244|PDB:4Y04}.
STRAND 658 660 {ECO:0000244|PDB:4Y04}.
STRAND 666 673 {ECO:0000244|PDB:4Y04}.
HELIX 675 681 {ECO:0000244|PDB:4Y04}.
TURN 686 688 {ECO:0000244|PDB:4Y04}.
STRAND 691 695 {ECO:0000244|PDB:4Y04}.
HELIX 696 705 {ECO:0000244|PDB:4Y04}.
HELIX 710 715 {ECO:0000244|PDB:4Y04}.
SEQUENCE 720 AA; 81938 MW; 95D117E5770CFF7D CRC64;
MKKRLLLPLF AALCLSQIAH ADEGMWLMQQ LGRKYAQMKE RGLKMKEYDL YNPNGTSLKD
AVVLFDGGCT GEVVSDRGLV LTNHHCGYDM IQAHSTLEHN YLENGFWAMR EADELPNKDI
SVVFIDKIED VTDYVKKELK AIKDPNSMDY LSPKYLQKLA DKKAGKNFSA KNPGLSVEIK
AFYGGNLYLM FTKKTYTDVR LVGAPPSSIG KFGADTDNWI WPRHTGDFSI FRIYADKNGN
PAPYSEDNVP LKPKRFFNIS LGGVQENDYA MIMGFPGTTH RYFTASEVDE WKSIDNDIRI
RMRDIRQGVM LREMLADPQI KIMYSAKYAA SQNAYKRAIG ANWAIKTRGL RQNKQAMQDR
LIAWGAKQGT PRYEEAVHEI DATVAKRADL RRRYWMIEEG IIRGIEFARS PIPTEDETKA
LQGNDASARK EAIDKIRTRY SKFANKDYSA EVDKKVAVAM LTEYLKEIPY ENLPLHLRLV
KDRFAGDVQA YVDDIFARSV FGSEAQFDAF AAVPSVEKLA EDPMVLFASS VFDEYRKLYN
ELRPYDDPIL RAQRTYIAGL LEMDGDQDQF PDANLTLRFT YGQVKGYSPR DNVYYGHQTT
LDGVMEKEDP DNWEFVVDPK LKAVYERKDF GRYADRSGRM PVAFCATTHT TGGNSGSPVM
NANGELIGLN FDRNWEGVGG DIQYLADYQR SIIVDIRYVL LVIDKVGGCQ RLLDEMNIVP


Related products :

Catalog number Product name Quantity
EIAAB11842 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,DPP2,DPP7,Homo sapiens,Human,QPP,Quiescent cell proline dipeptidase
EIAAB11839 Dipeptidyl peptidase IV-related protein 3,Dipeptidyl peptidase X,Dipeptidyl peptidase-like protein 2,DPL2,DPP X,DPP10,DPRP3,DPRP-3,Homo sapiens,Human,Inactive dipeptidyl peptidase 10,KIAA1492
EIAAB11843 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,Dpp2,Dpp7,Quiescent cell proline dipeptidase,Rat,Rattus norvegicus
EIAAB11844 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,Dpp2,Dpp7,Mouse,Mus musculus,Qpp,Quiescent cell proline dipeptidase
EIAAB11854 Dipeptidyl peptidase 9,Dipeptidyl peptidase IV-related protein 2,Dipeptidyl peptidase IX,Dipeptidyl peptidase-like protein 9,DP9,DPLP9,DPP IX,DPP9,DPRP2,DPRP-2,Homo sapiens,Human
EIAAB11845 Dipeptidyl aminopeptidase III,Dipeptidyl arylamidase III,Dipeptidyl peptidase 3,Dipeptidyl peptidase III,DPP III,DPP3,Homo sapiens,Human
EIAAB11855 Dipeptidyl peptidase 9,Dipeptidyl peptidase IX,Dipeptidyl peptidase-like protein 9,DP9,DPLP9,DPP IX,Dpp9,Mouse,Mus musculus
EIAAB11847 Dipeptidyl aminopeptidase III,Dipeptidyl arylamidase III,Dipeptidyl peptidase 3,Dipeptidyl peptidase III,DPP III,Dpp3,Rat,Rattus norvegicus
EIAAB11846 Dipeptidyl aminopeptidase III,Dipeptidyl arylamidase III,Dipeptidyl peptidase 3,Dipeptidyl peptidase III,DPP III,Dpp3,Mouse,Mus musculus
EIAAB11848 Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,Dpp6,DPPX,Rat,Rattus norve
EIAAB11849 Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,DPP6,DPPX,Homo sapiens,Hum
EIAAB11852 Dipeptidyl peptidase 8,Dipeptidyl peptidase IV-related protein 1,Dipeptidyl peptidase VIII,DP8,DPP VIII,DPP8,DPRP1,DPRP-1,Homo sapiens,Human,MSTP097,MSTP135,MSTP141,Prolyl dipeptidase DPP8
EIAAB11851 Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,Dpp6,Dpp-6,DPPX,Mouse,Mus
EIAAB11850 Bos taurus,Bovine,Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,DPP6,DPP
20-321-175240 DIPEPTIDYL PEPTIDASE IV (DPP IV). CD26 - MONOCLONAL ANTIBODY TO RAT DIPEPTIDYL PEPTIDASE IV (DPP IV). CD26; EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosi 0.1 mg
EIAAB05418 Cathepsin C,Cathepsin J,CPPI,CTSC,Dipeptidyl peptidase 1,Dipeptidyl peptidase I,Dipeptidyl transferase,DPPI,DPP-I,Homo sapiens,Human
E0884r ELISA kit Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD2 96T
EIAAB05420 Bos taurus,Bovine,Cathepsin C,Cathepsin J,CTSC,Dipeptidyl peptidase 1,Dipeptidyl peptidase I,Dipeptidyl transferase,DPPI,DPP-I
EIAAB05421 Cathepsin C,Cathepsin J,Ctsc,Dipeptidyl peptidase 1,Dipeptidyl peptidase I,Dipeptidyl transferase,DPPI,DPP-I,Mouse,Mus musculus
EIAAB05419 Cathepsin C,Cathepsin J,Ctsc,Dipeptidyl peptidase 1,Dipeptidyl peptidase I,Dipeptidyl transferase,DPPI,DPP-I,Rat,Rattus norvegicus
EIAAB11840 Dipeptidyl peptidase X,DPP X,Dpp10,Inactive dipeptidyl peptidase 10,Kv4 potassium channel auxiliary subunit,Rat,Rattus norvegicus
E0884r ELISA Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD26 96T
U0884r CLIA Bile canaliculus domain-specific membrane glycoprotein,Cd26,Dipeptidyl peptidase 4,Dipeptidyl peptidase IV,DPP IV,Dpp4,GP110 glycoprotein,Rat,Rattus norvegicus,T-cell activation antigen CD26 96T
15-288-21442 Dipeptidyl peptidase 4 - EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosine deaminase complexing protein 2; ADABP Polyclonal 0.1 mg
15-288-21442 Dipeptidyl peptidase 4 - EC 3.4.14.5; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; Adenosine deaminase complexing protein 2; ADABP Polyclonal 0.05 mg


 

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