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Beta-lactamase TEM (EC 3.5.2.6) (IRT-4) (Penicillinase) (TEM-1) (TEM-16/CAZ-7) (TEM-2) (TEM-24/CAZ-6) (TEM-3) (TEM-4) (TEM-5) (TEM-6) (TEM-8/CAZ-2)

 BLAT_ECOLX              Reviewed;         286 AA.
P62593; P00810; Q47313;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 109.
RecName: Full=Beta-lactamase TEM;
EC=3.5.2.6;
AltName: Full=IRT-4;
AltName: Full=Penicillinase;
AltName: Full=TEM-1;
AltName: Full=TEM-16/CAZ-7;
AltName: Full=TEM-2;
AltName: Full=TEM-24/CAZ-6;
AltName: Full=TEM-3;
AltName: Full=TEM-4;
AltName: Full=TEM-5;
AltName: Full=TEM-6;
AltName: Full=TEM-8/CAZ-2;
Flags: Precursor;
Name=bla;
and
Name=blaT-3;
and
Name=blaT-4;
and
Name=blaT-5;
and
Name=blaT-6;
Escherichia coli.
Plasmid R1 (R7268), Plasmid IncFII R100 (NR1), Plasmid R6K,
Plasmid pUD16, Plasmid pCFF04, and Plasmid pCFF14.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=562;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
PLASMID=R1 (R7268); TRANSPOSON=Tn3;
PubMed=358200; DOI=10.1073/pnas.75.8.3737;
Sutcliffe J.G.;
"Nucleotide sequence of the ampicillin resistance gene of Escherichia
coli plasmid pBR322.";
Proc. Natl. Acad. Sci. U.S.A. 75:3737-3741(1978).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
PLASMID=R1 (R7268); TRANSPOSON=Tn3;
PubMed=383387;
Sutcliffe J.G.;
"Complete nucleotide sequence of the Escherichia coli plasmid
pBR322.";
Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1979).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
PLASMID=IncFII R100 (NR1);
PubMed=3019092; DOI=10.1016/0065-227X(86)90018-3;
Ohtsubo H., Ryder T.B., Maeda Y., Armstrong K., Ohtsubo E.;
"DNA replication of the resistance plasmid R100 and its control.";
Adv. Biophys. 21:115-133(1986).
[4]
PROTEIN SEQUENCE OF 24-286 (TEM-2).
PLASMID=R6K; TRANSPOSON=Tn1;
PubMed=358199; DOI=10.1073/pnas.75.8.3732;
Ambler R.P., Scott G.K.;
"Partial amino acid sequence of penicillinase coded by Escherichia
coli plasmid R6K.";
Proc. Natl. Acad. Sci. U.S.A. 75:3732-3736(1978).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
Sougakoff W., Goussard S., Courvalin P.;
"The TEM-3 beta-lactamase, which hydrolyzes broad-spectrum
cephalosporins, is derived from the TEM-2 penicillinase by two amino
acid substitutions.";
FEMS Microbiol. Lett. 56:343-348(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
PLASMID=pCFF04;
PubMed=1331747; DOI=10.1007/BF00286188;
Mabilat C., Lourencao-Vital J., Goussard S., Courvalin P.;
"A new example of physical linkage between Tn1 and Tn21: the
antibiotic multiple-resistance region of plasmid pCFF04 encoding
extended-spectrum beta-lactamase TEM-3.";
Mol. Gen. Genet. 235:113-121(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-4 AND TEM-5).
STRAIN=CB86134; PLASMID=pCFF04, and pUD16;
PubMed=2550326; DOI=10.1016/0378-1119(89)90236-9;
Sougakoff W., Petit A., Goussard S., Sirot D., Bure A., Courvalin P.;
"Characterization of the plasmid genes blaT-4 and blaT-5 which encode
the broad-spectrum beta-lactamases TEM-4 and TEM-5 in
enterobacteriaceae.";
Gene 78:339-348(1989).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-6).
STRAIN=HB251;
PubMed=1665171; DOI=10.1099/00221287-137-12-2681;
Goussard S., Sougakoff W., Mabilat C., Bauernfeind A., Courvalin P.;
"An IS1-like element is responsible for high-level synthesis of
extended-spectrum beta-lactamase TEM-6 in Enterobacteriaceae.";
J. Gen. Microbiol. 137:2681-2687(1991).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-8; TEM-16 AND TEM-24).
PubMed=1416873; DOI=10.1128/AAC.36.9.1817;
Chanal C., Poupart M.C., Sirot D., Labia R., Sirot J., Cluzel R.;
"Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase
genes.";
Antimicrob. Agents Chemother. 36:1817-1820(1992).
[10]
PROTEIN SEQUENCE OF 24-286 (IRT-4).
STRAIN=PEY;
PubMed=8056282; DOI=10.1111/j.1574-6968.1994.tb07016.x;
Brun T., Peduzzi J., Canica M.M., Paul G., Nevot P., Barthelemy M.,
Labia R.;
"Characterization and amino acid sequence of IRT-4, a novel TEM-type
enzyme with a decreased susceptibility to beta-lactamase inhibitors.";
FEMS Microbiol. Lett. 120:111-117(1994).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF TEM-1.
PubMed=1544485; DOI=10.1016/0014-5793(92)80232-6;
Jelsch C., Lenfant F., Masson J.-M., Samama J.-P.;
"Beta-lactamase TEM1 of E. coli. Crystal structure determination at
2.5-A resolution.";
FEBS Lett. 299:135-142(1992).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF TEM-1.
PubMed=8356032; DOI=10.1002/prot.340160406;
Jelsch C., Mourey L., Masson J.-M., Samama J.-P.;
"Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8-A
resolution.";
Proteins 16:364-383(1993).
[13]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF TEM-1 COMPLEXED WITH BLIP.
PubMed=8605632; DOI=10.1038/nsb0396-290;
Strynadka N.C.J., Jensen S.E., Alzari P.M., James M.N.G.;
"A potent new mode of beta-lactamase inhibition revealed by the 1.7 A
X-ray crystallographic structure of the TEM-1-BLIP complex.";
Nat. Struct. Biol. 3:290-297(1996).
[14]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF TEM-1.
PubMed=9485412; DOI=10.1021/bi972501b;
Maveyraud L., Pratt R.F., Samama J.-P.;
"Crystal structure of an acylation transition-state analog of the TEM-
1 beta-lactamase. Mechanistic implications for class A beta-
lactamases.";
Biochemistry 37:2622-2628(1998).
[15]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF TEM-1.
PubMed=10423234; DOI=10.1021/bi990758z;
Swaren P., Golemi D., Cabantous S., Bulychev A., Maveyraud L.,
Mobashery S., Samama J.-P.;
"X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-
1 beta-lactamase: direct observation of electrostatic modulation in
resistance to inactivation by clavulanic acid.";
Biochemistry 38:9570-9576(1999).
-!- FUNCTION: TEM-type are the most prevalent beta-lactamases in
enterobacteria; they hydrolyze the beta-lactam bond in susceptible
beta-lactam antibiotics, thus conferring resistance to penicillins
and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing
cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing
ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and
aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly
active against ceftazidime. IRT-4 shows resistance to beta-
lactamase inhibitors.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000255|PROSITE-ProRule:PRU10101}.
-!- INTERACTION:
P35804:- (xeno); NbExp=2; IntAct=EBI-1031989, EBI-1031985;
-!- BIOTECHNOLOGY: This protein is used as a marker in many commonly
used cloning vectors, such as pBR322 and the pUC series.
-!- MISCELLANEOUS: The beta-lactamase present on pBR322 was cloned
from plasmid R1 (R7268).
-!- SIMILARITY: Belongs to the class-A beta-lactamase family.
{ECO:0000305}.
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EMBL; J01749; AAB59737.1; -; Genomic_DNA.
EMBL; V00613; CAA23886.1; -; Genomic_DNA.
EMBL; X64523; CAA45828.1; -; Genomic_DNA.
EMBL; X57972; CAA41038.1; -; Genomic_DNA.
EMBL; X65252; CAA46344.1; -; Genomic_DNA.
EMBL; X65253; CAA46345.1; -; Genomic_DNA.
EMBL; X65254; CAA46346.1; -; Genomic_DNA.
EMBL; U89928; AAB64386.1; -; Genomic_DNA.
EMBL; U66885; AAC48875.1; -; Genomic_DNA.
PIR; A93821; PNECP.
PIR; S30113; S30113.
RefSeq; NP_943295.1; NC_005248.1.
RefSeq; NP_957565.1; NC_005327.1.
RefSeq; WP_000027057.1; NZ_NQJA01000259.1.
RefSeq; WP_063864949.1; NG_050277.1.
RefSeq; YP_001096393.1; NC_009132.1.
RefSeq; YP_001693174.1; NC_010378.1.
RefSeq; YP_001816609.1; NC_010558.1.
RefSeq; YP_003108102.1; NC_013120.1.
RefSeq; YP_003108210.1; NC_013121.1.
RefSeq; YP_003829069.1; NC_014383.1.
RefSeq; YP_003829170.1; NC_014384.1.
RefSeq; YP_003937675.1; NC_014615.1.
RefSeq; YP_004119720.1; NC_014843.1.
RefSeq; YP_004119734.1; NC_014843.1.
RefSeq; YP_006903139.1; NC_019047.1.
RefSeq; YP_006939984.1; NC_018994.1.
RefSeq; YP_006940092.1; NC_018995.1.
RefSeq; YP_006952181.1; NC_019056.1.
RefSeq; YP_006952421.1; NC_019062.1.
RefSeq; YP_006952427.1; NC_019063.1.
RefSeq; YP_006953479.1; NC_019073.1.
RefSeq; YP_006953762.1; NC_019088.1.
RefSeq; YP_006953988.1; NC_019091.1.
RefSeq; YP_006954235.1; NC_019095.1.
RefSeq; YP_007447512.1; NC_020278.2.
RefSeq; YP_008864019.1; NC_022992.1.
RefSeq; YP_008864686.1; NC_022996.1.
RefSeq; YP_008995211.1; NC_023277.2.
RefSeq; YP_009060387.1; NC_024960.1.
RefSeq; YP_009060444.1; NC_024961.1.
RefSeq; YP_009060580.1; NC_024967.1.
RefSeq; YP_009061316.1; NC_024977.1.
RefSeq; YP_009066523.1; NC_025106.1.
RefSeq; YP_009068284.1; NC_025139.1.
RefSeq; YP_009068507.1; NC_025141.1.
RefSeq; YP_009070232.1; NC_025167.1.
RefSeq; YP_009070558.1; NC_025175.1.
RefSeq; YP_009071512.1; NC_025183.1.
RefSeq; YP_190222.1; NC_006671.1.
PDB; 1AXB; X-ray; 2.00 A; A=24-286.
PDB; 1BT5; X-ray; 1.80 A; A=24-286.
PDB; 1BTL; X-ray; 1.80 A; A=24-286.
PDB; 1CK3; X-ray; 2.28 A; A=24-284.
PDB; 1ERM; X-ray; 1.70 A; A=24-286.
PDB; 1ERO; X-ray; 2.10 A; A=24-286.
PDB; 1ERQ; X-ray; 1.90 A; A=24-286.
PDB; 1ESU; X-ray; 2.00 A; A=24-284.
PDB; 1FQG; X-ray; 1.70 A; A=24-286.
PDB; 1JTD; X-ray; 2.30 A; A=24-286.
PDB; 1JTG; X-ray; 1.73 A; A/C=24-286.
PDB; 1JVJ; X-ray; 1.73 A; A=24-286.
PDB; 1JWP; X-ray; 1.75 A; A=24-286.
PDB; 1JWV; X-ray; 1.85 A; A=24-286.
PDB; 1JWZ; X-ray; 1.80 A; A=24-286.
PDB; 1LHY; X-ray; 2.00 A; A=24-284.
PDB; 1LI0; X-ray; 1.61 A; A=24-284.
PDB; 1LI9; X-ray; 1.52 A; A=24-284.
PDB; 1M40; X-ray; 0.85 A; A=24-286.
PDB; 1NXY; X-ray; 1.60 A; A=24-286.
PDB; 1NY0; X-ray; 1.75 A; A=24-286.
PDB; 1NYM; X-ray; 1.20 A; A=24-286.
PDB; 1NYY; X-ray; 1.90 A; A=24-286.
PDB; 1PZO; X-ray; 1.90 A; A=24-284.
PDB; 1PZP; X-ray; 1.45 A; A=24-284.
PDB; 1S0W; X-ray; 2.30 A; A/B=24-286.
PDB; 1TEM; X-ray; 1.95 A; A=24-286.
PDB; 1XPB; X-ray; 1.90 A; A=24-286.
PDB; 1XXM; X-ray; 1.90 A; A/B=24-286.
PDB; 1YT4; X-ray; 1.40 A; A=24-284.
PDB; 1ZG4; X-ray; 1.55 A; A=1-284.
PDB; 1ZG6; X-ray; 2.10 A; A=1-284.
PDB; 2B5R; X-ray; 1.65 A; A/B=24-286.
PDB; 2V1Z; X-ray; 1.60 A; A=25-38, A=41-286.
PDB; 2V20; X-ray; 1.67 A; A=25-38, A=41-286.
PDB; 3C7U; X-ray; 2.20 A; A/C=24-286.
PDB; 3C7V; X-ray; 2.07 A; A/C=24-286.
PDB; 3CMZ; X-ray; 1.92 A; A=24-286.
PDB; 3DTM; X-ray; 2.00 A; A=24-286.
PDB; 3JYI; X-ray; 2.70 A; A/B/C/D/E/F=24-286.
PDB; 3TOI; X-ray; 1.90 A; A/B=39-283.
PDB; 4DXB; X-ray; 2.29 A; A/B=24-226.
PDB; 4DXC; X-ray; 2.30 A; A=24-226.
PDB; 4GKU; X-ray; 1.92 A; A=24-286.
PDB; 4IBR; X-ray; 2.20 A; A=24-286.
PDB; 4IBX; X-ray; 2.68 A; A/B/C/D/E=24-286.
PDB; 4ID4; X-ray; 1.05 A; A=24-147, A=189-286.
PDB; 4MEZ; X-ray; 2.05 A; A/B=24-286.
PDB; 4QY5; X-ray; 1.50 A; A=24-147, A=189-286.
PDB; 4QY6; X-ray; 1.15 A; A=24-147, A=189-286.
PDB; 4R4R; X-ray; 1.20 A; A=24-147, A=189-286.
PDB; 4R4S; X-ray; 1.10 A; A=24-149, A=189-286.
PDB; 4RVA; X-ray; 1.44 A; A=24-286.
PDB; 4RX2; X-ray; 2.31 A; A/B/C/D/E/F/G/H=24-286.
PDB; 4RX3; X-ray; 1.39 A; A=24-286.
PDB; 4ZJ1; X-ray; 1.54 A; A=1-286.
PDB; 4ZJ2; X-ray; 1.80 A; A=1-286.
PDB; 4ZJ3; X-ray; 1.70 A; A=1-286.
PDB; 5HVI; X-ray; 1.64 A; A/B/C/D=24-286.
PDB; 5HW1; X-ray; 1.70 A; A/B/C/D=24-286.
PDB; 5HW5; X-ray; 1.41 A; A/B/C/D=24-286.
PDB; 5I52; X-ray; 1.75 A; A/B/C/D=24-286.
PDB; 5I63; X-ray; 1.95 A; A/B/C/D=24-286.
PDB; 5IQ8; X-ray; 2.06 A; A/B/C/D=24-286.
PDB; 5KKF; X-ray; 1.82 A; A/B/C/D=24-286.
PDB; 5KPU; X-ray; 1.50 A; A/B/C/D=24-286.
PDBsum; 1AXB; -.
PDBsum; 1BT5; -.
PDBsum; 1BTL; -.
PDBsum; 1CK3; -.
PDBsum; 1ERM; -.
PDBsum; 1ERO; -.
PDBsum; 1ERQ; -.
PDBsum; 1ESU; -.
PDBsum; 1FQG; -.
PDBsum; 1JTD; -.
PDBsum; 1JTG; -.
PDBsum; 1JVJ; -.
PDBsum; 1JWP; -.
PDBsum; 1JWV; -.
PDBsum; 1JWZ; -.
PDBsum; 1LHY; -.
PDBsum; 1LI0; -.
PDBsum; 1LI9; -.
PDBsum; 1M40; -.
PDBsum; 1NXY; -.
PDBsum; 1NY0; -.
PDBsum; 1NYM; -.
PDBsum; 1NYY; -.
PDBsum; 1PZO; -.
PDBsum; 1PZP; -.
PDBsum; 1S0W; -.
PDBsum; 1TEM; -.
PDBsum; 1XPB; -.
PDBsum; 1XXM; -.
PDBsum; 1YT4; -.
PDBsum; 1ZG4; -.
PDBsum; 1ZG6; -.
PDBsum; 2B5R; -.
PDBsum; 2V1Z; -.
PDBsum; 2V20; -.
PDBsum; 3C7U; -.
PDBsum; 3C7V; -.
PDBsum; 3CMZ; -.
PDBsum; 3DTM; -.
PDBsum; 3JYI; -.
PDBsum; 3TOI; -.
PDBsum; 4DXB; -.
PDBsum; 4DXC; -.
PDBsum; 4GKU; -.
PDBsum; 4IBR; -.
PDBsum; 4IBX; -.
PDBsum; 4ID4; -.
PDBsum; 4MEZ; -.
PDBsum; 4QY5; -.
PDBsum; 4QY6; -.
PDBsum; 4R4R; -.
PDBsum; 4R4S; -.
PDBsum; 4RVA; -.
PDBsum; 4RX2; -.
PDBsum; 4RX3; -.
PDBsum; 4ZJ1; -.
PDBsum; 4ZJ2; -.
PDBsum; 4ZJ3; -.
PDBsum; 5HVI; -.
PDBsum; 5HW1; -.
PDBsum; 5HW5; -.
PDBsum; 5I52; -.
PDBsum; 5I63; -.
PDBsum; 5IQ8; -.
PDBsum; 5KKF; -.
PDBsum; 5KPU; -.
ProteinModelPortal; P62593; -.
SMR; P62593; -.
IntAct; P62593; 1.
BindingDB; P62593; -.
ChEMBL; CHEMBL2065; -.
DrugBank; DB08551; (1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC ACID.
DrugBank; DB07466; (1R)-2-PHENYLACETAMIDO-2-(3-CARBOXYPHENYL)ETHYL BORONIC ACID.
DrugBank; DB07464; 1(R)-1-ACETAMIDO-2-(3-CARBOXY-2-HYDROXYPHENYL)ETHYL BORONIC ACID.
DrugBank; DB02614; 1(R)-1-Acetamido-2-(3-Carboxyphenyl)Ethyl Boronic Acid.
DrugBank; DB04430; 3-(4-Phenylamino-Phenylamino)-2-(1h-Tetrazol-5-Yl)-Acrylonitrile.
DrugBank; DB07599; [(2-AMINO-ALPHA-METHOXYIMINO-4-THIAZOLYLACETYL)AMINO]METHYLBORONIC ACID.
DrugBank; DB02841; [(2-Ethoxy-1-Naphthoyl)Amino]Methylboronic Acid.
DrugBank; DB02642; [[N-(Benzyloxycarbonyl)Amino]Methyl]Phosphate.
DrugBank; DB09060; Avibactam.
DrugBank; DB01053; Benzylpenicillin.
DrugBank; DB04035; Pinacol[[2-Amino-Alpha-(1-Carboxy-1-Methylethoxyimino)-4-Thiazoleacetyl]Amino]Methaneboronate.
PRIDE; P62593; -.
GeneID; 10076131; -.
GeneID; 10076142; -.
GeneID; 13876868; -.
GeneID; 13877052; -.
GeneID; 13903673; -.
GeneID; 13905334; -.
GeneID; 13905363; -.
GeneID; 13906404; -.
GeneID; 13906709; -.
GeneID; 13906924; -.
GeneID; 13909533; -.
GeneID; 13909568; -.
GeneID; 14612524; -.
GeneID; 17824300; -.
GeneID; 17824435; -.
GeneID; 18157686; -.
GeneID; 20466965; -.
GeneID; 20466993; -.
GeneID; 20467118; -.
GeneID; 20468340; -.
GeneID; 20471961; -.
GeneID; 20491414; -.
GeneID; 20491639; -.
GeneID; 20492529; -.
GeneID; 20492626; -.
GeneID; 20493584; -.
GeneID; 2716540; -.
GeneID; 3244915; -.
GeneID; 33952196; -.
GeneID; 3722457; -.
GeneID; 4924718; -.
GeneID; 5961992; -.
GeneID; 6276043; -.
GeneID; 8319064; -.
GeneID; 8319163; -.
GeneID; 9537966; -.
GeneID; 9538101; -.
GeneID; 9846067; -.
KEGG; ag:AAB59737; -.
KEGG; ag:CAA41038; -.
KEGG; ag:CAA45828; -.
KEGG; ag:CAA46344; -.
KEGG; ag:CAA46345; -.
KEGG; ag:CAA46346; -.
KO; K18698; -.
BRENDA; 3.5.2.6; 2026.
SABIO-RK; P62593; -.
EvolutionaryTrace; P62593; -.
PRO; PR:P62593; -.
GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR000871; Beta-lactam_class-A.
InterPro; IPR023650; Beta-lactam_class-A_AS.
PRINTS; PR00118; BLACTAMASEA.
SUPFAM; SSF56601; SSF56601; 1.
PROSITE; PS00146; BETA_LACTAMASE_A; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Direct protein sequencing;
Disulfide bond; Hydrolase; Plasmid; Signal; Transposable element.
SIGNAL 1 23 {ECO:0000269|PubMed:358199,
ECO:0000269|PubMed:8056282}.
CHAIN 24 286 Beta-lactamase TEM.
/FTId=PRO_0000016978.
REGION 232 234 Substrate binding.
ACT_SITE 68 68 Acyl-ester intermediate.
ACT_SITE 166 166 Proton acceptor.
DISULFID 75 121
VARIANT 19 19 L -> F (in TEM-4).
VARIANT 37 37 Q -> K (in TEM-2, TEM-3, TEM-8, TEM-16
and TEM-24).
VARIANT 67 67 M -> L (in IRT-4).
VARIANT 102 102 E -> K (in TEM-3, TEM-4, TEM-6, TEM-8,
TEM-16 and TEM-24).
VARIANT 162 162 R -> H (in TEM-6 and TEM-16).
VARIANT 162 162 R -> S (in TEM-5, TEM-8 and TEM-24).
VARIANT 235 235 A -> T (in TEM-5 and TEM-24).
VARIANT 236 236 G -> S (in TEM-3, TEM-4 and TEM-8).
VARIANT 237 237 E -> K (in TEM-5 and TEM-24).
VARIANT 261 261 T -> M (in TEM-4).
VARIANT 272 272 N -> D (in IRT-4).
HELIX 25 38 {ECO:0000244|PDB:1M40}.
STRAND 40 48 {ECO:0000244|PDB:1M40}.
TURN 49 51 {ECO:0000244|PDB:1M40}.
STRAND 54 59 {ECO:0000244|PDB:1M40}.
HELIX 67 69 {ECO:0000244|PDB:1M40}.
HELIX 70 83 {ECO:0000244|PDB:1M40}.
HELIX 97 99 {ECO:0000244|PDB:1M40}.
HELIX 107 109 {ECO:0000244|PDB:1M40}.
TURN 111 113 {ECO:0000244|PDB:1M40}.
HELIX 117 126 {ECO:0000244|PDB:1M40}.
HELIX 130 139 {ECO:0000244|PDB:1M40}.
HELIX 143 152 {ECO:0000244|PDB:1M40}.
HELIX 166 168 {ECO:0000244|PDB:1M40}.
TURN 171 173 {ECO:0000244|PDB:1JWZ}.
HELIX 181 193 {ECO:0000244|PDB:1M40}.
STRAND 194 197 {ECO:0000244|PDB:4RX3}.
HELIX 199 210 {ECO:0000244|PDB:1M40}.
STRAND 213 215 {ECO:0000244|PDB:1PZP}.
TURN 216 218 {ECO:0000244|PDB:1M40}.
HELIX 219 222 {ECO:0000244|PDB:1M40}.
STRAND 228 235 {ECO:0000244|PDB:1M40}.
TURN 237 239 {ECO:0000244|PDB:3TOI}.
STRAND 241 249 {ECO:0000244|PDB:1M40}.
STRAND 255 263 {ECO:0000244|PDB:1M40}.
HELIX 268 284 {ECO:0000244|PDB:1M40}.
SEQUENCE 286 AA; 31515 MW; BB678943BB18934B CRC64;
MSIQHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN SGKILESFRP
EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL VEYSPVTEKH LTDGMTVREL
CSAAITMSDN TAANLLLTTI GGPKELTAFL HNMGDHVTRL DRWEPELNEA IPNDERDTTM
PAAMATTLRK LLTGELLTLA SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS
RGIIAALGPD GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW


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