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

Endonuclease 8 (DNA glycosylase/AP lyase Nei) (EC 3.2.2.-) (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site) lyase Nei) (Endonuclease VIII)

 END8_ECOLI              Reviewed;         263 AA.
P50465;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 159.
RecName: Full=Endonuclease 8;
AltName: Full=DNA glycosylase/AP lyase Nei;
EC=3.2.2.-;
EC=4.2.99.18;
AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Nei;
AltName: Full=Endonuclease VIII;
Name=nei; OrderedLocusNames=b0714, JW0704;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-36;
189-206 AND 214-227.
PubMed=9171429; DOI=10.1128/jb.179.11.3773-3782.1997;
Jiang D., Hatahet Z., Blaisdell J.O., Melamede R.J., Wallace S.S.;
"Escherichia coli endonuclease VIII: cloning, sequencing, and
overexpression of the nei structural gene and characterization of nei
and nei nth mutants.";
J. Bacteriol. 179:3773-3782(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9171430; DOI=10.1128/jb.179.11.3783-3785.1997;
Saito Y., Uraki F., Nakajima S., Asaeda A., Ono K., Kubo K.,
Yamamoto K.;
"Characterization of endonuclease III (nth) and endonuclease VIII
(nei) mutants of Escherichia coli K-12.";
J. Bacteriol. 179:3783-3785(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[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]
MUTAGENESIS OF PRO-2; GLU-3; GLU-6; ASP-129; ASP-160 AND GLU-174.
PubMed=11711552; DOI=10.1074/jbc.M110499200;
Burgess S., Jaruga P., Dodson M.L., Dizdaroglu M., Lloyd R.S.;
"Determination of active site residues in Escherichia coli
endonuclease VIII.";
J. Biol. Chem. 277:2938-2944(2002).
[7]
FUNCTION, AND SUBSTRATES.
PubMed=20031487; DOI=10.1016/j.dnarep.2009.11.008;
Guo Y., Bandaru V., Jaruga P., Zhao X., Burrows C.J., Iwai S.,
Dizdaroglu M., Bond J.P., Wallace S.S.;
"The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit
different substrate preferences from their Escherichia coli
counterparts.";
DNA Repair 9:177-190(2010).
[8]
X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEX WITH DNA, AND
MUTAGENESIS OF GLU-3; LYS-53; ARG-213 AND ARG-253.
PubMed=11847126; DOI=10.1093/emboj/21.4.789;
Zharkov D.O., Golan G., Gilboa R., Fernandes A.S., Gerchman S.E.,
Kycia J.H., Rieger R.A., Grollman A.P., Shoham G.;
"Structural analysis of an Escherichia coli endonuclease VIII covalent
reaction intermediate.";
EMBO J. 21:789-800(2002).
-!- FUNCTION: Involved in base excision repair of DNA damaged by
oxidation or by mutagenic agents. Acts as DNA glycosylase that
recognizes and removes damaged bases. Has a preference for
oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil
and 5,6-dihydrothymine. Acts on DNA bubble and 3'-fork structures,
suggesting a role in replication-associated DNA repair. Has AP
(apurinic/apyrimidinic) lyase activity and introduces nicks in the
DNA strand. Cleaves the DNA backbone by beta-delta elimination to
generate a single-strand break at the site of the removed base
with both 3'- and 5'-phosphates. {ECO:0000269|PubMed:20031487}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U38616; AAC45355.1; -; Genomic_DNA.
EMBL; D89754; BAA20414.1; -; Genomic_DNA.
EMBL; U00096; AAC73808.1; -; Genomic_DNA.
EMBL; AP009048; BAA35378.1; -; Genomic_DNA.
PIR; A64807; A64807.
RefSeq; NP_415242.1; NC_000913.3.
RefSeq; WP_001113989.1; NZ_LN832404.1.
PDB; 1K3W; X-ray; 1.42 A; A=2-263.
PDB; 1K3X; X-ray; 1.25 A; A=2-263.
PDB; 1Q39; X-ray; 2.80 A; A=2-263.
PDB; 1Q3B; X-ray; 2.05 A; A=2-263.
PDB; 1Q3C; X-ray; 2.30 A; A=2-263.
PDB; 2EA0; X-ray; 1.40 A; A=2-263.
PDB; 2OPF; X-ray; 1.85 A; A=2-263.
PDB; 2OQ4; X-ray; 2.60 A; A/B=2-263.
PDBsum; 1K3W; -.
PDBsum; 1K3X; -.
PDBsum; 1Q39; -.
PDBsum; 1Q3B; -.
PDBsum; 1Q3C; -.
PDBsum; 2EA0; -.
PDBsum; 2OPF; -.
PDBsum; 2OQ4; -.
DisProt; DP00375; -.
ProteinModelPortal; P50465; -.
SMR; P50465; -.
BioGrid; 4259928; 110.
DIP; DIP-10327N; -.
IntAct; P50465; 13.
STRING; 316385.ECDH10B_0781; -.
PaxDb; P50465; -.
PRIDE; P50465; -.
EnsemblBacteria; AAC73808; AAC73808; b0714.
EnsemblBacteria; BAA35378; BAA35378; BAA35378.
GeneID; 945320; -.
KEGG; ecj:JW0704; -.
KEGG; eco:b0714; -.
PATRIC; fig|1411691.4.peg.1559; -.
EchoBASE; EB3026; -.
EcoGene; EG13237; nei.
eggNOG; ENOG4108S0J; Bacteria.
eggNOG; COG0266; LUCA.
HOGENOM; HOG000020882; -.
InParanoid; P50465; -.
KO; K05522; -.
OMA; EILWQAQ; -.
PhylomeDB; P50465; -.
BioCyc; EcoCyc:G6383-MONOMER; -.
BioCyc; MetaCyc:G6383-MONOMER; -.
BRENDA; 3.2.2.23; 2026.
BRENDA; 4.2.99.18; 2026.
EvolutionaryTrace; P50465; -.
PRO; PR:P50465; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0140080; F:class III/IV DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0003684; F:damaged DNA binding; IDA:EcoliWiki.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:EcoliWiki.
GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
GO; GO:0006284; P:base-excision repair; IDA:EcoliWiki.
GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
Gene3D; 3.20.190.10; -; 1.
HAMAP; MF_01253; Endonuclease_8; 1.
InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
InterPro; IPR023713; Endonuclease-VIII.
InterPro; IPR012319; FPG_cat.
InterPro; IPR035937; MutM-like_N-ter.
InterPro; IPR010979; Ribosomal_S13-like_H2TH.
InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
InterPro; IPR010663; Znf_FPG/IleRS.
Pfam; PF01149; Fapy_DNA_glyco; 1.
Pfam; PF06831; H2TH; 1.
Pfam; PF06827; zf-FPG_IleRS; 1.
SMART; SM00898; Fapy_DNA_glyco; 1.
SMART; SM01232; H2TH; 1.
SUPFAM; SSF46946; SSF46946; 1.
SUPFAM; SSF81624; SSF81624; 1.
PROSITE; PS51068; FPG_CAT; 1.
PROSITE; PS01242; ZF_FPG_1; 1.
PROSITE; PS51066; ZF_FPG_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
Metal-binding; Multifunctional enzyme; Reference proteome; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9171429}.
CHAIN 2 263 Endonuclease 8.
/FTId=PRO_0000170893.
ZN_FING 229 263 FPG-type.
ACT_SITE 2 2 Schiff-base intermediate with DNA.
ACT_SITE 3 3 Proton donor. {ECO:0000305}.
ACT_SITE 53 53 Proton donor; for beta-elimination
activity. {ECO:0000305}.
ACT_SITE 253 253 Proton donor; for delta-elimination
activity. {ECO:0000305}.
BINDING 70 70 DNA. {ECO:0000269|PubMed:11847126}.
BINDING 125 125 DNA. {ECO:0000269|PubMed:11847126}.
BINDING 169 169 DNA. {ECO:0000269|PubMed:11847126}.
MUTAGEN 2 2 P->T: Loss of glycosylase and AP lyase
activity. {ECO:0000269|PubMed:11711552}.
MUTAGEN 3 3 E->A,Q: Loss of glycosylase activity. No
effect on AP lyase activity.
{ECO:0000269|PubMed:11711552,
ECO:0000269|PubMed:11847126}.
MUTAGEN 3 3 E->D: Much reduced glycosylase activity.
No effect on AP lyase activity.
{ECO:0000269|PubMed:11711552,
ECO:0000269|PubMed:11847126}.
MUTAGEN 6 6 E->Q: Reduced glycosylase activity. No
effect on AP lyase activity.
{ECO:0000269|PubMed:11711552}.
MUTAGEN 53 53 K->A: Loss of DNA cleavage at sites
containing oxidized pyrimidine. No effect
on AP lyase activity.
{ECO:0000269|PubMed:11847126}.
MUTAGEN 129 129 D->N: Reduced glycosylase activity. No
effect on AP lyase activity.
{ECO:0000269|PubMed:11711552}.
MUTAGEN 160 160 D->N: No effect on glycosylase and AP
lyase activity.
{ECO:0000269|PubMed:11711552}.
MUTAGEN 174 174 E->Q: Loss of glycosylase activity. No
effect on AP lyase activity.
{ECO:0000269|PubMed:11711552}.
MUTAGEN 213 213 R->A: Slightly reduced activity.
{ECO:0000269|PubMed:11847126}.
MUTAGEN 253 253 R->A: Reduced DNA cleavage at sites
containing oxidized pyrimidine. No effect
on AP lyase activity.
{ECO:0000269|PubMed:11847126}.
HELIX 4 18 {ECO:0000244|PDB:1K3X}.
STRAND 24 30 {ECO:0000244|PDB:1K3X}.
HELIX 31 35 {ECO:0000244|PDB:1K3X}.
HELIX 36 40 {ECO:0000244|PDB:1K3X}.
STRAND 45 51 {ECO:0000244|PDB:1K3X}.
STRAND 54 59 {ECO:0000244|PDB:1K3X}.
STRAND 64 68 {ECO:0000244|PDB:1K3X}.
TURN 70 72 {ECO:0000244|PDB:1K3X}.
STRAND 74 79 {ECO:0000244|PDB:1K3X}.
STRAND 90 95 {ECO:0000244|PDB:1K3X}.
STRAND 97 105 {ECO:0000244|PDB:1K3X}.
STRAND 108 112 {ECO:0000244|PDB:1K3X}.
HELIX 116 119 {ECO:0000244|PDB:1K3X}.
HELIX 121 125 {ECO:0000244|PDB:1K3X}.
HELIX 137 145 {ECO:0000244|PDB:1K3X}.
TURN 147 151 {ECO:0000244|PDB:1K3X}.
HELIX 154 157 {ECO:0000244|PDB:1K3X}.
TURN 161 163 {ECO:0000244|PDB:1K3X}.
HELIX 169 179 {ECO:0000244|PDB:1K3X}.
HELIX 187 189 {ECO:0000244|PDB:1K3X}.
HELIX 192 212 {ECO:0000244|PDB:1K3X}.
TURN 213 215 {ECO:0000244|PDB:2OPF}.
HELIX 218 220 {ECO:0000244|PDB:1Q3B}.
STRAND 229 232 {ECO:0000244|PDB:1Q3C}.
TURN 239 241 {ECO:0000244|PDB:1K3X}.
STRAND 246 250 {ECO:0000244|PDB:1K3X}.
STRAND 253 257 {ECO:0000244|PDB:1K3X}.
TURN 259 261 {ECO:0000244|PDB:1K3X}.
SEQUENCE 263 AA; 29845 MW; 7D10B79F58ADDA24 CRC64;
MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF PQLKPYQSQL IGQHVTHVET RGKALLTHFS
NDLTLYSHNQ LYGVWRVVDT GEEPQTTRVL RVKLQTADKT ILLYSASDIE MLTPEQLTTH
PFLQRVGPDV LDPNLTPEVV KERLLSPRFR NRQFAGLLLD QAFLAGLGNY LRVEILWQVG
LTGNHKAKDL NAAQLDALAH ALLEIPRFSY ATRGQVDENK HHGALFRFKV FHRDGEPCER
CGSIIEKTTL SSRPFYWCPG CQH


Related products :

Catalog number Product name Quantity
EIAAB26876 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,Mouse,Mus musculus,NEH1,Nei homolog 1,Nei1,Neil1,Nei-like protein 1
EIAAB26878 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Gm1212,Mouse,Mus musculus,NEH2,Nei homolog 2,Neil2,Nei-like protein 2
EIAAB26879 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Homo sapiens,Human,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26880 Bos taurus,Bovine,DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26877 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,FPG1,Homo sapiens,Human,NEH1,Nei homolog 1,NEIL1,Nei-like protein 1
18-003-43959 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
18-003-43958 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
18-003-43422 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN; Protein REF-1 Polyclonal 0.1 mg Protein A
EIAAB26881 DNA glycosylase FPG2,DNA glycosylase_AP lyase Neil3,Endonuclease 8-like 3,Endonuclease VIII-like 3,Mouse,Mus musculus,Neil3,Nei-like protein 3
EIAAB26883 DNA glycosylase FPG2,DNA glycosylase_AP lyase Neil3,Endonuclease 8-like 3,Endonuclease VIII-like 3,Homo sapiens,Human,NEIL3,Nei-like protein 3
EH2009 DNA-(apurinic or apyrimidinic site) lyase Elisa Kit 96T
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase 500ug
AE56100RA Rat DNA- (apurinic or apyrimidinic site) lyase (APEX1) ELISA Kit 48T
E14887d Mouse ELISA Kit FOR DNA-(apurinic or apyrimidinic site) lyase 2 96T
CSB-EL001900RA Rat DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001901BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
abx109730 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody 100 μg
CSB-EL001900BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
abx108186 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (HRP) 100 μg
CSB-EL001900HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001901MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EL001900MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001901HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
abx105348 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (Biotin) 100 μg
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase Source: E.coli 200ug


 

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