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

Proofreading thioesterase EntH (EC 3.1.2.-) (Enterobactin synthase component H) (p15)

 ENTH_ECOLI              Reviewed;         137 AA.
P0A8Y8; P15050; Q2MBK4;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 1.
28-MAR-2018, entry version 97.
RecName: Full=Proofreading thioesterase EntH {ECO:0000255|HAMAP-Rule:MF_00907};
EC=3.1.2.- {ECO:0000255|HAMAP-Rule:MF_00907};
AltName: Full=Enterobactin synthase component H {ECO:0000255|HAMAP-Rule:MF_00907};
AltName: Full=p15;
Name=entH {ECO:0000255|HAMAP-Rule:MF_00907,
ECO:0000303|PubMed:17675380}; Synonyms=ybdB;
OrderedLocusNames=b0597, JW0589;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2521621;
Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.;
"Nucleotide sequence and transcriptional organization of the
Escherichia coli enterobactin biosynthesis cistrons entB and entA.";
J. Bacteriol. 171:784-790(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2521622;
Liu J., Duncan K., Walsh C.T.;
"Nucleotide sequence of a cluster of Escherichia coli enterobactin
biosynthesis genes: identification of entA and purification of its
product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase.";
J. Bacteriol. 171:791-798(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
FUNCTION AS AN ESTERASE.
PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
"Enzyme genomics: application of general enzymatic screens to discover
new enzymes.";
FEMS Microbiol. Rev. 29:263-279(2005).
[7]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, INTERACTION WITH
ENTB, SUBCELLULAR LOCATION, INDUCTION, AND GENE NAME.
STRAIN=K12;
PubMed=17675380; DOI=10.1128/JB.00755-07;
Leduc D., Battesti A., Bouveret E.;
"The hotdog thioesterase EntH (YbdB) plays a role in vivo in optimal
enterobactin biosynthesis by interacting with the ArCP domain of
EntB.";
J. Bacteriol. 189:7112-7126(2007).
[8]
FUNCTION AS AN ESTERASE, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19119850; DOI=10.1021/bi802207t;
Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.;
"In vitro kinetic analysis of substrate specificity in enterobactin
biosynthetic lower pathway enzymes provides insight into the
biochemical function of the hot dog-fold thioesterase EntH.";
Biochemistry 48:511-513(2009).
[9]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, AND
MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
STRAIN=K12;
PubMed=19193103; DOI=10.1021/bi802165x;
Guo Z.F., Sun Y., Zheng S., Guo Z.;
"Preferential hydrolysis of aberrant intermediates by the type II
thioesterase in Escherichia coli nonribosomal enterobactin synthesis:
substrate specificities and mutagenic studies on the active-site
residues.";
Biochemistry 48:1712-1722(2009).
[10]
FUNCTION, AND MUTAGENESIS OF MET-68.
PubMed=24992697; DOI=10.1021/bi500333m;
Latham J.A., Chen D., Allen K.N., Dunaway-Mariano D.;
"Divergence of substrate specificity and function in the Escherichia
coli hotdog-fold thioesterase paralogs YdiI and YbdB.";
Biochemistry 53:4775-4787(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-137.
Murshudov G.N., Vagin A.A., Dodson E.J.;
"Crystal structure of a putative thioesterase.";
Submitted (DEC-2003) to the PDB data bank.
[12]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE
ANALOGS, SUBUNIT, MUTAGENESIS OF GLN-48; HIS-54; GLU-63 AND MET-68,
AND ACTIVE SITE.
PubMed=25010423; DOI=10.1021/bi500334v;
Wu R., Latham J.A., Chen D., Farelli J., Zhao H., Matthews K.,
Allen K.N., Dunaway-Mariano D.;
"Structure and catalysis in the Escherichia coli hotdog-fold
thioesterase paralogs YdiI and YbdB.";
Biochemistry 53:4788-4805(2014).
-!- FUNCTION: Required for optimal enterobactin synthesis. Acts as a
proofreading enzyme that prevents EntB misacylation by hydrolyzing
the thioester bound existing between EntB and wrongly charged
molecules. Displays esterase activity toward a wide range of
substrates, including acyl-CoAs and aryl-CoAs.
{ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:17675380,
ECO:0000269|PubMed:19119850, ECO:0000269|PubMed:19193103,
ECO:0000269|PubMed:24992697}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=16 uM for 2,3-DHB-EntB {ECO:0000269|PubMed:19119850};
KM=116 uM for 2,3-DHB-EntB {ECO:0000269|PubMed:19193103};
KM=21 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19119850};
KM=190 uM for 4-hydroxybenzoyl-CoA
{ECO:0000269|PubMed:19193103};
KM=25 uM for 2,4-DHB-EntB {ECO:0000269|PubMed:19119850};
KM=32 uM for lauroyl-EntB {ECO:0000269|PubMed:19119850};
KM=35 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19119850};
KM=265 uM for 3-hydroxybenzoyl-CoA
{ECO:0000269|PubMed:19193103};
KM=37 uM for 3-HPA-CoA {ECO:0000269|PubMed:19119850};
KM=45 uM for lauroyl-CoA {ECO:0000269|PubMed:19119850};
KM=49 uM for decanoyl-CoA {ECO:0000269|PubMed:19119850};
KM=55 uM for palmitoyl-CoA {ECO:0000269|PubMed:19119850};
KM=4.25 uM for palmitoyl-CoA {ECO:0000269|PubMed:19193103};
KM=161 uM for 2,3-dihydroxybenzoyl-CoA
{ECO:0000269|PubMed:19193103};
KM=176 uM for salicylyl-CoA {ECO:0000269|PubMed:19193103};
KM=212 uM for 3,4-dihydroxybenzoyl-CoA
{ECO:0000269|PubMed:19193103};
KM=219 uM for 2,4-dihydroxybenzoyl-CoA
{ECO:0000269|PubMed:19193103};
KM=256 uM for 3,5-dihydroxybenzoyl-CoA
{ECO:0000269|PubMed:19193103};
KM=272 uM for salicylyl-EntB {ECO:0000269|PubMed:19193103};
KM=350 uM for hexanoyl-CoA {ECO:0000269|PubMed:19119850};
KM=400 uM for propionyl-CoA {ECO:0000269|PubMed:19119850};
KM=475 uM for benzoyl-CoA {ECO:0000269|PubMed:19193103};
KM=800 uM for acetyl-CoA {ECO:0000269|PubMed:19119850};
-!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000269|PubMed:17675380}.
-!- SUBUNIT: Homotetramer. Dimer of dimers. Interacts specifically
with the aryl carrier protein (ArCP) domain of EntB.
{ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000269|PubMed:17675380,
ECO:0000269|PubMed:19193103, ECO:0000269|PubMed:25010423}.
-!- INTERACTION:
P0ADI4:entB; NbExp=3; IntAct=EBI-1118982, EBI-547993;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00907,
ECO:0000269|PubMed:17675380}.
-!- INDUCTION: Induced by iron starvation.
{ECO:0000269|PubMed:17675380}.
-!- SIMILARITY: Belongs to the thioesterase PaaI family.
{ECO:0000255|HAMAP-Rule:MF_00907}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M24148; AAA16104.1; -; Unassigned_DNA.
EMBL; M24143; AAA76837.1; -; Genomic_DNA.
EMBL; U82598; AAB40797.1; -; Genomic_DNA.
EMBL; U00096; AAC73698.1; -; Genomic_DNA.
EMBL; AP009048; BAE76352.1; -; Genomic_DNA.
PIR; B91904; Q3ECEA.
RefSeq; NP_415129.1; NC_000913.3.
RefSeq; WP_000637953.1; NZ_LN832404.1.
PDB; 1VH9; X-ray; 2.15 A; A/B=2-137.
PDB; 4K4C; X-ray; 1.85 A; A/B/C/D=1-137.
PDB; 4K4D; X-ray; 2.17 A; A/B=1-137.
PDBsum; 1VH9; -.
PDBsum; 4K4C; -.
PDBsum; 4K4D; -.
ProteinModelPortal; P0A8Y8; -.
SMR; P0A8Y8; -.
BioGrid; 4260982; 15.
DIP; DIP-11343N; -.
IntAct; P0A8Y8; 2.
STRING; 316385.ECDH10B_0665; -.
EPD; P0A8Y8; -.
PaxDb; P0A8Y8; -.
PRIDE; P0A8Y8; -.
EnsemblBacteria; AAC73698; AAC73698; b0597.
EnsemblBacteria; BAE76352; BAE76352; BAE76352.
GeneID; 945215; -.
KEGG; ecj:JW0589; -.
KEGG; eco:b0597; -.
PATRIC; fig|1411691.4.peg.1672; -.
EchoBASE; EB1097; -.
EcoGene; EG11105; entH.
eggNOG; ENOG4108TZA; Bacteria.
eggNOG; COG2050; LUCA.
HOGENOM; HOG000066991; -.
InParanoid; P0A8Y8; -.
OMA; HGGVYCS; -.
PhylomeDB; P0A8Y8; -.
BioCyc; EcoCyc:EG11105-MONOMER; -.
BioCyc; MetaCyc:EG11105-MONOMER; -.
BRENDA; 3.1.2.2; 2026.
UniPathway; UPA00017; -.
EvolutionaryTrace; P0A8Y8; -.
PRO; PR:P0A8Y8; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016289; F:CoA hydrolase activity; IDA:EcoCyc.
GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0016790; F:thiolester hydrolase activity; IDA:EcoCyc.
GO; GO:0009239; P:enterobactin biosynthetic process; IMP:EcoCyc.
HAMAP; MF_00907; Thioesterase_EntH; 1.
InterPro; IPR029069; HotDog_dom_sf.
InterPro; IPR003736; PAAI_dom.
InterPro; IPR026576; Thioesterase_EntH.
InterPro; IPR006683; Thioestr_dom.
Pfam; PF03061; 4HBT; 1.
SUPFAM; SSF54637; SSF54637; 1.
TIGRFAMs; TIGR00369; unchar_dom_1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Hydrolase;
Reference proteome.
CHAIN 1 137 Proofreading thioesterase EntH.
/FTId=PRO_0000156676.
REGION 54 55 Substrate binding.
{ECO:0000269|PubMed:25010423}.
REGION 89 92 Substrate binding.
{ECO:0000269|PubMed:25010423}.
ACT_SITE 63 63 Nucleophile or proton acceptor.
{ECO:0000255|HAMAP-Rule:MF_00907,
ECO:0000303|PubMed:25010423,
ECO:0000305|PubMed:19193103}.
BINDING 48 48 Substrate. {ECO:0000269|PubMed:25010423}.
BINDING 82 82 Substrate; via carbonyl oxygen.
{ECO:0000269|PubMed:25010423}.
MUTAGEN 48 48 Q->A: Loss of activity.
{ECO:0000269|PubMed:19193103,
ECO:0000269|PubMed:25010423}.
MUTAGEN 48 48 Q->N: 290-fold decrease in activity
toward salicylyl-CoA.
{ECO:0000269|PubMed:19193103}.
MUTAGEN 54 54 H->A: 229-fold decrease in activity
toward salicylyl-CoA. Loss of activity
toward benzoyl-CoA.
{ECO:0000269|PubMed:19193103,
ECO:0000269|PubMed:25010423}.
MUTAGEN 63 63 E->A,D,Q: Loss of activity.
{ECO:0000269|PubMed:19193103,
ECO:0000269|PubMed:25010423}.
MUTAGEN 64 64 T->S: 13-fold decrease in activity toward
salicylyl-CoA.
{ECO:0000269|PubMed:19193103}.
MUTAGEN 67 67 S->A: 140-fold decrease in activity
toward salicylyl-CoA.
{ECO:0000269|PubMed:19193103}.
MUTAGEN 67 67 S->C: 104-fold decrease in activity
toward salicylyl-CoA.
{ECO:0000269|PubMed:19193103}.
MUTAGEN 68 68 M->A: 130-fold decrease in activity
toward salicylyl-CoA.
{ECO:0000269|PubMed:19193103}.
MUTAGEN 68 68 M->V: 47-fold increase in catalytic
efficiency toward 1,4-dihydroxy-2-
naphthoyl-CoA and 10-fold increase in
catalytic efficiency toward lauroyl-CoA.
Does not affect catalytic efficiency
toward benzoyl-CoA.
{ECO:0000269|PubMed:24992697,
ECO:0000269|PubMed:25010423}.
HELIX 9 14 {ECO:0000244|PDB:4K4C}.
TURN 15 18 {ECO:0000244|PDB:4K4C}.
HELIX 20 23 {ECO:0000244|PDB:4K4C}.
STRAND 27 31 {ECO:0000244|PDB:4K4C}.
STRAND 36 41 {ECO:0000244|PDB:4K4C}.
TURN 44 46 {ECO:0000244|PDB:4K4C}.
STRAND 51 53 {ECO:0000244|PDB:4K4C}.
HELIX 55 71 {ECO:0000244|PDB:4K4C}.
STRAND 79 89 {ECO:0000244|PDB:4K4C}.
STRAND 95 107 {ECO:0000244|PDB:4K4C}.
STRAND 109 119 {ECO:0000244|PDB:4K4C}.
STRAND 125 136 {ECO:0000244|PDB:4K4C}.
SEQUENCE 137 AA; 14970 MW; C8DF8DE63815F206 CRC64;
MIWKRHLTLD ELNATSDNTM VAHLGIVYTR LGDDVLEAEM PVDTRTHQPF GLLHGGASAA
LAETLGSMAG FMMTRDGQCV VGTELNATHH RPVSEGKVRG VCQPLHLGRQ NQSWEIVVFD
EQGRRCCTCR LGTAVLG


Related products :

Catalog number Product name Quantity
EIAAB37319 Mouse,Mus musculus,Olah,Oleoyl-ACP hydrolase,S-acyl fatty acid synthase thioesterase, medium chain,Thedc1,Thioesterase domain-containing protein 1,Thioesterase II
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
EIAAB37320 Augmented in rheumatoid arthritis 1,AURA1,Homo sapiens,Human,OLAH,Oleoyl-ACP hydrolase,S-acyl fatty acid synthase thioesterase, medium chain,THEDC1,Thioesterase domain-containing protein 1,Thioesteras
MCA5591Z MOUSE ANTI HUMAN ENTH Azide free, Product Type Monoclonal Antibody, Specificity ENTH, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applications WB, Clone 1E6 0.1 mg
PCR-237L Pfu_X Core Kit, L pack Kit of proofreading DNA polymerase for highest accuracy, dNTPs and reaction bufferKit of proofreading DNA polymerase for highest accuracy, dNTPs and reaction buffer 500units
PCR-237L Pfu_X Core Kit, L pack Kit of proofreading DNA polymerase for highest accuracy, dNTPs and reaction bufferKit of proofreading DNA polymerase for highest accuracy, dNTPs and reaction buffer 500 units
G8653 S-acyl fatty acid synthase thioesterase, medium chain (OLAH), Rat, ELISA Kit 96T
SAST_MOUSE Mouse ELISA Kit FOR S-acyl fatty acid synthase thioesterase, medium chain 96T
CSB-EL016319RA Rat S-acyl fatty acid synthase thioesterase, medium chain(OLAH) ELISA kit 96T
G8651 S-acyl fatty acid synthase thioesterase, medium chain (OLAH), Human, ELISA Kit 96T
CSB-EL016319RA Rat S-acyl fatty acid synthase thioesterase, medium chain(OLAH) ELISA kit SpeciesRat 96T
G8652 S-acyl fatty acid synthase thioesterase, medium chain (OLAH), Mouse, ELISA Kit 96T
CSB-EL016319HU Human S-acyl fatty acid synthase thioesterase, medium chain(OLAH) ELISA kit 96T
CSB-EL016319MO Mouse S-acyl fatty acid synthase thioesterase, medium chain(OLAH) ELISA kit 96T
PCR-237L Pfu-X Core Kit, L pack Kit of proofreading DNA polymerase for highest accuracy, dNTPs and reaction bufferKit of proofreading DNA polymerase for highest accuracy, dNTPs and reaction buffer 500units
25-595 ATP5G2 is a subunit of mitochondrial ATP synthase. ATP synthase is composed of two linked multi-subunit complexes the soluble catalytic core, F1, and the membrane-spanning component, F0, comprising t 0.05 mg
CSB-EL016319MO Mouse S-acyl fatty acid synthase thioesterase, medium chain(OLAH) ELISA kit SpeciesMouse 96T
SAST_RAT ELISA Kit FOR S-acyl fatty acid synthase thioesterase, medium chain; organism: Rat; gene name: Olah 96T
CSB-EL016319HU Human S-acyl fatty acid synthase thioesterase, medium chain(OLAH) ELISA kit SpeciesHuman 96T
SAST_MOUSE ELISA Kit FOR S-acyl fatty acid synthase thioesterase, medium chain; organism: Mouse; gene name: Olah 96T
EIAAB32136 Homo sapiens,Human,Lysosomal thioesterase PPT2,PPT2,PPT-2,S-thioesterase G14
orb37100 ENTH antibody 5 ug(Trial size)
orb37100 ENTH antibody 100 ug
YF-MA11197 anti-ENTH (1E6) 100 ug
orb37100 ENTH antibody 20 ug(Trial size)


 

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