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 1 (DNA glycosylase/AP lyase Nei 1) (EC 3.2.2.-) (DNA-(apurinic or apyrimidinic site) lyase Nei 1) (EC 4.2.99.18) (Endonuclease VIII 1)

 END8A_MYCTU             Reviewed;         268 AA.
P9WNB9; L0TCL5; O53191; P64158;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
23-MAY-2018, entry version 26.
RecName: Full=Endonuclease 8 1;
AltName: Full=DNA glycosylase/AP lyase Nei 1;
EC=3.2.2.-;
AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Nei 1;
EC=4.2.99.18;
AltName: Full=Endonuclease VIII 1;
Name=nei1; Synonyms=nei2; OrderedLocusNames=Rv2464c;
ORFNames=MTV008.20c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION, AND DNA-BINDING.
STRAIN=36KAZ;
PubMed=18457574; DOI=10.1134/S0006297908040093;
Sidorenko V.S., Rot M.A., Filipenko M.L., Nevinsky G.A., Zharkov D.O.;
"Novel DNA glycosylases from Mycobacterium tuberculosis.";
Biochemistry (Mosc.) 73:442-450(2008).
[3]
INDUCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19496823; DOI=10.1111/j.1574-695X.2009.00562.x;
Olsen I., Balasingham S.V., Davidsen T., Debebe E., Rodland E.A.,
van Soolingen D., Kremer K., Alseth I., Tonjum T.;
"Characterization of the major formamidopyrimidine-DNA glycosylase
homolog in Mycobacterium tuberculosis and its linkage to variable
tandem repeats.";
FEMS Immunol. Med. Microbiol. 56:151-161(2009).
[4]
FUNCTION, AND SUBSTRATES.
STRAIN=ATCC 25618 / H37Rv;
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[6]
REVIEW.
PubMed=21764637; DOI=10.1016/j.tube.2011.06.005;
Kurthkoti K., Varshney U.;
"Base excision and nucleotide excision repair pathways in
mycobacteria.";
Tuberculosis 91:533-543(2011).
-!- FUNCTION: Involved in base excision repair of DNA damaged by
oxidation or by mutagenic agents. DNA glycosylase that recognizes
and removes damaged pyrimidines. Excises Tg:A (thymine glycol,
prefers 5R isomers), Tg:G, 5,6-dihydrouracil:G base pairs and
urea:A, also excises oxidized purine derivatives
guanidinohydantoin:C and spiroiminodihydantoin:C. Poorly cleaves
dsDNA with uracil substitutions, thus also acting as a weak
uracil-DNA glycosylase. Acts on DNA bubble and 3'-fork structures,
suggesting a role in replication-associated DNA repair. Activity
on 7,8-dihydro-8-oxoguanine (8-oxoG) is debated; a report shows
weak activity (PubMed:18457574), whereas another shows none
(PubMed:20031487). Has AP (apurinic/apyrimidinic) activity and
introduces nicks in dsDNA strand, inefficiently cleaves ssDNA with
AP sites and uracil. Probably 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. Cleaves ssDNA
containing an AP site. Complements an E.coli fpg mutY but not nei
nth double mutant (PubMed:18457574). {ECO:0000269|PubMed:18457574,
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;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00391};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00391};
-!- INDUCTION: Expressed in mid-log phase.
{ECO:0000269|PubMed:19496823}.
-!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}.
-!- CAUTION: There are 2 paralogs in M.tuberculosis, in some
references this gene is called nei2 (PubMed:18457574 and
PubMed:19496823). {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL123456; CCP45257.1; -; Genomic_DNA.
PIR; G70865; G70865.
RefSeq; NP_216980.1; NC_000962.3.
RefSeq; WP_003412657.1; NZ_KK339370.1.
ProteinModelPortal; P9WNB9; -.
SMR; P9WNB9; -.
STRING; 83332.Rv2464c; -.
PaxDb; P9WNB9; -.
EnsemblBacteria; CCP45257; CCP45257; Rv2464c.
GeneID; 888500; -.
KEGG; mtu:Rv2464c; -.
TubercuList; Rv2464c; -.
eggNOG; ENOG4105CY4; Bacteria.
eggNOG; COG0266; LUCA.
KO; K05522; -.
OMA; MGRPPRV; -.
PhylomeDB; P9WNB9; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:MTBBASE.
GO; GO:0003690; F:double-stranded DNA binding; IDA:MTBBASE.
GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IDA:MTBBASE.
GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IDA:MTBBASE.
GO; GO:0003697; F:single-stranded DNA binding; IDA:MTBBASE.
GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:MTBBASE.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006284; P:base-excision repair; IEA:InterPro.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:MTBBASE.
GO; GO:0006281; P:DNA repair; IDA:MTBBASE.
GO; GO:0006289; P:nucleotide-excision repair; IMP:MTBBASE.
GO; GO:0006979; P:response to oxidative stress; IDA:MTBBASE.
Gene3D; 3.20.190.10; -; 1.
InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
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; PS01242; ZF_FPG_1; 1.
PROSITE; PS51066; ZF_FPG_2; 1.
1: Evidence at protein level;
Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase;
Hydrolase; Lyase; Metal-binding; Multifunctional enzyme;
Reference proteome; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 268 Endonuclease 8 1.
/FTId=PRO_0000170903.
ZN_FING 234 268 FPG-type. {ECO:0000255|PROSITE-
ProRule:PRU00391}.
ACT_SITE 2 2 Schiff-base intermediate with DNA.
{ECO:0000250}.
ACT_SITE 3 3 Proton donor. {ECO:0000250}.
ACT_SITE 52 52 Proton donor; for beta-elimination
activity. {ECO:0000250}.
ACT_SITE 258 258 Proton donor; for delta-elimination
activity. {ECO:0000250}.
BINDING 125 125 DNA. {ECO:0000250}.
BINDING 166 166 DNA. {ECO:0000250}.
SEQUENCE 268 AA; 29714 MW; 1142DE185BD14F24 CRC64;
MPEGHTLHRL ARLHQRRFAG APVSVSSPQG RFADSASALN GRVLRRASAW GKHLFHHYVG
GPVVHVHLGL YGTFTEWARP TDGWLPEPAG QVRMRMVGAE FGTDLRGPTV CESIDDGEVA
DVVARLGPDP LRSDANPSSA WSRITKSRRP IGALLMDQTV IAGVGNVYRN ELLFRHRIDP
QRPGRGIGEP EFDAAWNDLV SLMKVGLRRG KIIVVRPEHD HGLPSYLPDR PRTYVYRRAG
EPCRVCGGVI RTALLEGRNV FWCPVCQT


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