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Lysozyme C (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C)

 LYSC_HUMAN              Reviewed;         148 AA.
P61626; P00695; Q13170; Q9UCF8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
28-MAR-2018, entry version 158.
RecName: Full=Lysozyme C;
EC=3.2.1.17;
AltName: Full=1,4-beta-N-acetylmuramidase C;
Flags: Precursor;
Name=LYZ; Synonyms=LZM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2971592; DOI=10.1016/0378-1119(88)90359-9;
Castanon M.J., Spevak W., Adolf G.R., Chlebowicz-Sledziewska E.,
Sledziewski A.;
"Cloning of human lysozyme gene and expression in the yeast
Saccharomyces cerevisiae.";
Gene 66:223-234(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3413092; DOI=10.1073/pnas.85.17.6227;
Chung L.P., Keshav S., Gordon S.;
"Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and
in situ hybridization for macrophages and Paneth cells.";
Proc. Natl. Acad. Sci. U.S.A. 85:6227-6231(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2829884; DOI=10.1016/0006-291X(88)90461-5;
Yoshimura K., Toibana A., Nakahama K.;
"Human lysozyme: sequencing of a cDNA, and expression and secretion by
Saccharomyces cerevisiae.";
Biochem. Biophys. Res. Commun. 150:794-801(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2546758; DOI=10.1111/j.1432-1033.1989.tb14857.x;
Peters C.W.B., Kruse U., Pollwein R., Grzeschik K.H., Sippel A.E.;
"The human lysozyme gene. Sequence organization and chromosomal
localization.";
Eur. J. Biochem. 182:507-516(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Huang B., Zhao C., Lei X., Cai L.;
"The cloning, sequencing and analysis of Chinese human lysozyme gene
cDNA amplified with RT-PCR from human placental total RNA.";
Sheng Wu Hua Hsueh Tsa Chih 9:269-273(1993).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 19-148.
TISSUE=Urine;
PubMed=5284421;
Canfield R.E., Kammerman S., Sobel H.H., Morgan F.J.;
"Primary structure of lysozymes from man and goose.";
Nature New Biol. 232:16-17(1971).
[8]
PROTEIN SEQUENCE OF 19-148, AND SEQUENCE REVISION TO 118.
TISSUE=Urine;
PubMed=11946554; DOI=10.1016/0014-5793(72)80212-6;
Thomsen J., Lund E.H., Kristiansen K., Brunfeldt K., Malmquist J.;
"A Val-Val sequence found in a human monocytic leukemia lysozyme.";
FEBS Lett. 22:34-36(1972).
[9]
PROTEIN SEQUENCE OF 19-148.
TISSUE=Milk;
PubMed=5168859; DOI=10.1002/hlca.19710540830;
Jolles J., Jolles P.;
"Human milk lysozyme: unpublished data concerning the establishment of
the complete primary structure; comparison with lysozymes of various
origins.";
Helv. Chim. Acta 54:2668-2675(1971).
[10]
PROTEIN SEQUENCE OF 19-148, AND SEQUENCE REVISION TO 118.
TISSUE=Milk;
PubMed=11946553; DOI=10.1016/0014-5793(72)80211-4;
Jolles J., Jolles P.;
"Comparison between human and bird lysozymes: note concerning the
previously observed deletion.";
FEBS Lett. 22:31-33(1972).
[11]
PROTEIN SEQUENCE OF 19-41 AND 96-148, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Tear;
PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
Suarez T., Elortza F.;
"Human basal tear peptidome characterization by CID, HCD, and ETD
followed by in silico and in vitro analyses for antimicrobial peptide
identification.";
J. Proteome Res. 14:2649-2658(2015).
[12]
FOLDING, AND MUTAGENESIS.
PubMed=8503881; DOI=10.1042/bj2920469;
Kanaya E., Ishihara K., Tsunasawa S., Nokihara K., Kikuchi M.;
"Indication of possible post-translational formation of disulphide
bonds in the beta-sheet domain of human lysozyme.";
Biochem. J. 292:469-476(1993).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Banyard S.H., Blake C.C.F., Swan I.D.A.;
"The high resolution X-ray study of human. lysozyme: a preliminary
analysis.";
(In) Osserman E.F., Canfield R.E., Beychok S. (eds.);
Lysozyme, pp.71-79, Academic Press, New York (1974).
[16]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed=7334520; DOI=10.1016/0022-2836(81)90125-X;
Artymiuk P.J., Blake C.C.F.;
"Refinement of human lysozyme at 1.5-A resolution analysis of non-
bonded and hydrogen-bond interactions.";
J. Mol. Biol. 152:737-762(1981).
[17]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed=6876162; DOI=10.1016/S0022-2836(83)80105-3;
Blake C.C.F., Pulford W.C.A., Artymiuk P.J.;
"X-ray studies of water in crystals of lysozyme.";
J. Mol. Biol. 167:693-723(1983).
[18]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-99 AND ALA-113.
PubMed=2061330;
Inaka K., Taniyama Y., Kikuchi M., Morikawa K., Matsushima M.;
"The crystal structure of a mutant human lysozyme C77/95A with
increased secretion efficiency in yeast.";
J. Biol. Chem. 266:12599-12603(1991).
[19]
X-RAY CRYSTALLOGRAPHY (1.6 AND 1.1 ANGSTROMS).
PubMed=9757091; DOI=10.1107/S0907444997016922;
Steinrauf L.K.;
"Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic
lysozyme nitrate at 1.1 A.";
Acta Crystallogr. D 54:767-780(1998).
[20]
STRUCTURE BY NMR.
PubMed=2207098; DOI=10.1021/bi00483a007;
Redfield C., Dobson C.M.;
"1H NMR studies of human lysozyme: spectral assignment and comparison
with hen lysozyme.";
Biochemistry 29:7201-7214(1990).
[21]
STRUCTURE BY NMR.
PubMed=1794972;
Ohkubo T., Taniyama Y., Kikuchi M.;
"1H and 15N NMR study of human lysozyme.";
J. Biochem. 110:1022-1029(1991).
[22]
VARIANTS AMYL8 THR-74 AND HIS-85.
PubMed=8464497; DOI=10.1038/362553a0;
Pepy M.B., Hawkins P.N., Booth D.R., Vigushin D.M., Tennent G.A.,
Soutar A.K., Totty N., Nguyen O., Blake C.C.F., Terry C.J.,
Feest T.G., Zalin A.M., Hsuan J.J.;
"Human lysozyme gene mutations cause hereditary systemic
amyloidosis.";
Nature 362:553-557(1993).
-!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those
in tissues and body fluids are associated with the monocyte-
macrophage system and enhance the activity of immunoagents.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
acetylmuramic acid and N-acetyl-D-glucosamine residues in a
peptidoglycan and between N-acetyl-D-glucosamine residues in
chitodextrins.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-355360, EBI-355360;
-!- SUBCELLULAR LOCATION: Secreted.
-!- DISEASE: Amyloidosis 8 (AMYL8) [MIM:105200]: A form of hereditary
generalized amyloidosis. Clinical features include extensive
visceral amyloid deposits, renal amyloidosis resulting in
nephrotic syndrome, arterial hypertension, hepatosplenomegaly,
cholestasis, petechial skin rash. There is no involvement of the
nervous system. {ECO:0000269|PubMed:8464497}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
transglycosylation; it shows also a slight esterase activity. It
acts rapidly on both peptide-substituted and unsubstituted
peptidoglycan, and slowly on chitin oligosaccharides.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
{ECO:0000255|PROSITE-ProRule:PRU00680}.
-!- SEQUENCE CAUTION:
Sequence=CAA32175.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Lysozyme entry;
URL="https://en.wikipedia.org/wiki/Lysozyme";
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EMBL; M21119; AAA36188.1; -; mRNA.
EMBL; J03801; AAA59535.1; -; mRNA.
EMBL; M19045; AAA59536.1; -; mRNA.
EMBL; X14008; CAA32175.1; ALT_INIT; Genomic_DNA.
EMBL; U25677; AAC63078.1; -; mRNA.
EMBL; BC004147; AAH04147.1; -; mRNA.
CCDS; CCDS8989.1; -.
PIR; S04938; LZHU.
RefSeq; NP_000230.1; NM_000239.2.
UniGene; Hs.524579; -.
PDB; 133L; X-ray; 1.77 A; A=19-148.
PDB; 134L; X-ray; 1.77 A; A=19-148.
PDB; 1B5U; X-ray; 1.80 A; A=19-148.
PDB; 1B5V; X-ray; 2.17 A; A=19-148.
PDB; 1B5W; X-ray; 2.17 A; A=19-148.
PDB; 1B5X; X-ray; 2.00 A; A=19-148.
PDB; 1B5Y; X-ray; 2.20 A; A=19-148.
PDB; 1B5Z; X-ray; 2.20 A; A/B=19-148.
PDB; 1B7L; X-ray; 1.80 A; A=19-148.
PDB; 1B7M; X-ray; 2.20 A; A=19-148.
PDB; 1B7N; X-ray; 1.80 A; A=19-148.
PDB; 1B7O; X-ray; 1.80 A; A=19-148.
PDB; 1B7P; X-ray; 2.00 A; A=19-148.
PDB; 1B7Q; X-ray; 2.00 A; A=19-148.
PDB; 1B7R; X-ray; 1.80 A; A=19-148.
PDB; 1B7S; X-ray; 2.00 A; A=19-148.
PDB; 1BB3; X-ray; 1.80 A; A/B=19-148.
PDB; 1BB4; X-ray; 2.23 A; A/B=19-148.
PDB; 1BB5; X-ray; 1.80 A; A/B=19-148.
PDB; 1C43; X-ray; 1.80 A; A=19-148.
PDB; 1C45; X-ray; 1.80 A; A=19-148.
PDB; 1C46; X-ray; 2.20 A; A=19-148.
PDB; 1C7P; X-ray; 2.40 A; A=16-148.
PDB; 1CJ6; X-ray; 1.80 A; A=19-148.
PDB; 1CJ7; X-ray; 1.80 A; A=19-148.
PDB; 1CJ8; X-ray; 1.80 A; A=19-148.
PDB; 1CJ9; X-ray; 1.80 A; A=19-148.
PDB; 1CKC; X-ray; 1.80 A; A=19-148.
PDB; 1CKD; X-ray; 1.80 A; A=19-148.
PDB; 1CKF; X-ray; 1.80 A; A=19-148.
PDB; 1CKG; X-ray; 2.20 A; A/B=19-148.
PDB; 1CKH; X-ray; 2.00 A; A=19-148.
PDB; 1D6P; X-ray; 2.23 A; A=19-148.
PDB; 1D6Q; X-ray; 1.96 A; A=19-148.
PDB; 1DI3; X-ray; 1.80 A; A=19-148.
PDB; 1DI4; X-ray; 2.00 A; A=19-148.
PDB; 1DI5; X-ray; 2.20 A; A=19-148.
PDB; 1EQ4; X-ray; 1.80 A; A=19-148.
PDB; 1EQ5; X-ray; 1.80 A; A=19-148.
PDB; 1EQE; X-ray; 1.80 A; A=19-148.
PDB; 1GAY; X-ray; 1.80 A; A=19-148.
PDB; 1GAZ; X-ray; 1.80 A; A=19-148.
PDB; 1GB0; X-ray; 1.80 A; A=19-148.
PDB; 1GB2; X-ray; 1.80 A; A=19-148.
PDB; 1GB3; X-ray; 1.80 A; A=19-148.
PDB; 1GB5; X-ray; 1.80 A; A=19-148.
PDB; 1GB6; X-ray; 1.80 A; A=19-148.
PDB; 1GB7; X-ray; 1.80 A; A=19-148.
PDB; 1GB8; X-ray; 1.80 A; A=19-148.
PDB; 1GB9; X-ray; 1.80 A; A=19-148.
PDB; 1GBO; X-ray; 1.80 A; A=19-148.
PDB; 1GBW; X-ray; 1.80 A; A=19-148.
PDB; 1GBX; X-ray; 1.80 A; A=19-148.
PDB; 1GBY; X-ray; 1.80 A; A=19-148.
PDB; 1GBZ; X-ray; 1.80 A; A=19-148.
PDB; 1GDW; X-ray; 1.80 A; A=19-148.
PDB; 1GDX; X-ray; 1.80 A; A=19-148.
PDB; 1GE0; X-ray; 1.80 A; A=19-148.
PDB; 1GE1; X-ray; 1.70 A; A=19-148.
PDB; 1GE2; X-ray; 2.00 A; A=19-148.
PDB; 1GE3; X-ray; 1.80 A; A=19-148.
PDB; 1GE4; X-ray; 1.80 A; A=19-148.
PDB; 1GEV; X-ray; 2.10 A; A=19-148.
PDB; 1GEZ; X-ray; 1.80 A; A=19-148.
PDB; 1GF0; X-ray; 1.80 A; A=19-148.
PDB; 1GF3; X-ray; 1.80 A; A=19-148.
PDB; 1GF4; X-ray; 1.80 A; A=19-148.
PDB; 1GF5; X-ray; 1.80 A; A=19-148.
PDB; 1GF6; X-ray; 1.80 A; A=19-148.
PDB; 1GF7; X-ray; 1.80 A; A=19-148.
PDB; 1GF8; X-ray; 1.80 A; A=19-148.
PDB; 1GF9; X-ray; 1.80 A; A=19-148.
PDB; 1GFA; X-ray; 1.80 A; A=19-148.
PDB; 1GFE; X-ray; 1.80 A; A=19-148.
PDB; 1GFG; X-ray; 1.80 A; A=19-148.
PDB; 1GFH; X-ray; 1.80 A; A=19-148.
PDB; 1GFJ; X-ray; 1.80 A; A=19-148.
PDB; 1GFK; X-ray; 1.80 A; A=19-148.
PDB; 1GFR; X-ray; 1.80 A; A=19-148.
PDB; 1GFT; X-ray; 1.80 A; A=19-148.
PDB; 1GFU; X-ray; 1.80 A; A=19-148.
PDB; 1GFV; X-ray; 1.80 A; A=19-148.
PDB; 1HNL; X-ray; 1.80 A; A=19-148.
PDB; 1I1Z; X-ray; 1.80 A; A=19-148.
PDB; 1I20; X-ray; 1.90 A; A=19-148.
PDB; 1I22; X-ray; 1.80 A; A/B/C/D=19-148.
PDB; 1INU; X-ray; 1.80 A; A=19-148.
PDB; 1IOC; X-ray; 2.40 A; A=19-148.
PDB; 1IP1; X-ray; 1.80 A; A=19-148.
PDB; 1IP2; X-ray; 1.80 A; A=19-148.
PDB; 1IP3; X-ray; 1.80 A; A/B=19-148.
PDB; 1IP4; X-ray; 1.80 A; A=19-148.
PDB; 1IP5; X-ray; 1.80 A; A=19-148.
PDB; 1IP6; X-ray; 1.80 A; A=19-148.
PDB; 1IP7; X-ray; 1.90 A; A/B=19-146.
PDB; 1IWT; X-ray; 1.40 A; A=19-148.
PDB; 1IWU; X-ray; 1.40 A; A=19-148.
PDB; 1IWV; X-ray; 1.40 A; A=19-148.
PDB; 1IWW; X-ray; 1.40 A; A=19-148.
PDB; 1IWX; X-ray; 1.40 A; A=19-148.
PDB; 1IWY; X-ray; 1.40 A; A=19-148.
PDB; 1IWZ; X-ray; 1.48 A; A=19-148.
PDB; 1IX0; X-ray; 1.80 A; A=19-148.
PDB; 1IY3; NMR; -; A=19-148.
PDB; 1IY4; NMR; -; A=19-148.
PDB; 1JKA; X-ray; 1.66 A; A=19-148.
PDB; 1JKB; X-ray; 1.66 A; A=19-148.
PDB; 1JKC; X-ray; 1.60 A; A=19-148.
PDB; 1JKD; X-ray; 1.80 A; A=19-148.
PDB; 1JSF; X-ray; 1.15 A; A=19-148.
PDB; 1JWR; X-ray; 1.40 A; A=19-148.
PDB; 1LAA; X-ray; 1.77 A; A=19-148.
PDB; 1LHH; X-ray; 1.80 A; A=19-148.
PDB; 1LHI; X-ray; 1.80 A; A=19-148.
PDB; 1LHJ; X-ray; 1.80 A; A=19-148.
PDB; 1LHK; X-ray; 1.80 A; A=19-148.
PDB; 1LHL; X-ray; 1.80 A; A=19-148.
PDB; 1LHM; X-ray; 1.80 A; A=19-148.
PDB; 1LMT; X-ray; 1.60 A; A=19-148.
PDB; 1LOZ; X-ray; 1.80 A; A=19-148.
PDB; 1LYY; X-ray; 1.80 A; A=19-148.
PDB; 1LZ1; X-ray; 1.50 A; A=19-148.
PDB; 1LZ4; X-ray; 1.80 A; A=19-148.
PDB; 1LZ5; X-ray; 1.80 A; A=19-144.
PDB; 1LZ6; X-ray; 1.80 A; A=19-140.
PDB; 1LZR; X-ray; 1.50 A; A=19-148.
PDB; 1LZS; X-ray; 1.60 A; A/B=19-148.
PDB; 1OP9; X-ray; 1.86 A; B=19-148.
PDB; 1OUA; X-ray; 1.80 A; A=19-148.
PDB; 1OUB; X-ray; 1.80 A; A=19-148.
PDB; 1OUC; X-ray; 1.80 A; A=19-148.
PDB; 1OUD; X-ray; 1.80 A; A=19-148.
PDB; 1OUE; X-ray; 1.80 A; A=19-148.
PDB; 1OUF; X-ray; 1.80 A; A=19-147.
PDB; 1OUG; X-ray; 1.80 A; A=19-148.
PDB; 1OUH; X-ray; 1.80 A; A=19-148.
PDB; 1OUI; X-ray; 1.80 A; A=19-148.
PDB; 1OUJ; X-ray; 1.80 A; A=19-148.
PDB; 1QSW; X-ray; 1.85 A; A/B/C/D=19-148.
PDB; 1RE2; X-ray; 2.30 A; A=19-148.
PDB; 1REM; X-ray; 2.10 A; A=19-148.
PDB; 1REX; X-ray; 1.50 A; A=19-148.
PDB; 1REY; X-ray; 1.70 A; A=19-148.
PDB; 1REZ; X-ray; 1.70 A; A=19-148.
PDB; 1TAY; X-ray; 1.70 A; A=19-148.
PDB; 1TBY; X-ray; 1.77 A; A=19-148.
PDB; 1TCY; X-ray; 1.70 A; A=19-148.
PDB; 1TDY; X-ray; 1.70 A; A=19-148.
PDB; 1UBZ; X-ray; 2.00 A; A=19-148.
PDB; 1W08; X-ray; 2.50 A; A=19-148.
PDB; 1WQM; X-ray; 1.80 A; A=19-148.
PDB; 1WQN; X-ray; 1.80 A; A=19-148.
PDB; 1WQO; X-ray; 1.80 A; A=19-148.
PDB; 1WQP; X-ray; 1.80 A; A=19-148.
PDB; 1WQQ; X-ray; 1.80 A; A=19-148.
PDB; 1WQR; X-ray; 1.80 A; A=19-148.
PDB; 1YAM; X-ray; 1.80 A; A=19-148.
PDB; 1YAN; X-ray; 1.80 A; A=19-148.
PDB; 1YAO; X-ray; 1.80 A; A=19-148.
PDB; 1YAP; X-ray; 1.80 A; A=19-148.
PDB; 1YAQ; X-ray; 1.80 A; A=19-148.
PDB; 207L; X-ray; 1.80 A; A=19-148.
PDB; 208L; X-ray; 2.20 A; A=19-148.
PDB; 2BQA; X-ray; 1.80 A; A=19-148.
PDB; 2BQB; X-ray; 1.80 A; A=19-148.
PDB; 2BQC; X-ray; 1.80 A; A=19-148.
PDB; 2BQD; X-ray; 1.80 A; A=19-148.
PDB; 2BQE; X-ray; 1.80 A; A=19-148.
PDB; 2BQF; X-ray; 1.80 A; A=19-148.
PDB; 2BQG; X-ray; 1.80 A; A=19-148.
PDB; 2BQH; X-ray; 1.80 A; A=19-148.
PDB; 2BQI; X-ray; 1.80 A; A=19-148.
PDB; 2BQJ; X-ray; 1.80 A; A=19-148.
PDB; 2BQK; X-ray; 1.80 A; A=19-147.
PDB; 2BQL; X-ray; 1.80 A; A=19-148.
PDB; 2BQM; X-ray; 1.80 A; A=19-148.
PDB; 2BQN; X-ray; 1.80 A; A=19-148.
PDB; 2BQO; X-ray; 1.80 A; A=19-148.
PDB; 2HEA; X-ray; 1.80 A; A=19-148.
PDB; 2HEB; X-ray; 2.20 A; A=19-148.
PDB; 2HEC; X-ray; 1.80 A; A=19-148.
PDB; 2HED; X-ray; 1.80 A; A=19-148.
PDB; 2HEE; X-ray; 1.80 A; A=19-148.
PDB; 2HEF; X-ray; 1.80 A; A=19-148.
PDB; 2LHM; X-ray; 1.80 A; A=19-148.
PDB; 2MEA; X-ray; 2.20 A; A/B=19-148.
PDB; 2MEB; X-ray; 1.80 A; A=19-148.
PDB; 2MEC; X-ray; 2.20 A; A/B=19-148.
PDB; 2MED; X-ray; 1.80 A; A=19-148.
PDB; 2MEE; X-ray; 1.80 A; A=19-148.
PDB; 2MEF; X-ray; 1.80 A; A=19-148.
PDB; 2MEG; X-ray; 1.80 A; A=19-148.
PDB; 2MEH; X-ray; 1.80 A; A=19-148.
PDB; 2MEI; X-ray; 1.80 A; A=19-148.
PDB; 2NWD; X-ray; 1.04 A; X=19-148.
PDB; 2ZIJ; X-ray; 1.90 A; A=19-148.
PDB; 2ZIK; X-ray; 1.81 A; A=19-148.
PDB; 2ZIL; X-ray; 1.80 A; A=19-148.
PDB; 2ZWB; Neutron; 1.80 A; A=19-148.
PDB; 3EBA; X-ray; 1.85 A; B=19-148.
PDB; 3FE0; X-ray; 1.50 A; A=19-148.
PDB; 3LHM; X-ray; 1.80 A; A=19-148.
PDB; 3LN2; X-ray; 2.04 A; A/B=19-148.
PDB; 4I0C; X-ray; 1.95 A; A/B=19-148.
PDB; 4ML7; X-ray; 1.80 A; A/C=19-148.
PDB; 4R0P; X-ray; 1.52 A; A=74-79.
PDB; 5LSH; X-ray; 1.06 A; A=19-148.
PDB; 5LVK; X-ray; 2.49 A; A/B=19-148.
PDBsum; 133L; -.
PDBsum; 134L; -.
PDBsum; 1B5U; -.
PDBsum; 1B5V; -.
PDBsum; 1B5W; -.
PDBsum; 1B5X; -.
PDBsum; 1B5Y; -.
PDBsum; 1B5Z; -.
PDBsum; 1B7L; -.
PDBsum; 1B7M; -.
PDBsum; 1B7N; -.
PDBsum; 1B7O; -.
PDBsum; 1B7P; -.
PDBsum; 1B7Q; -.
PDBsum; 1B7R; -.
PDBsum; 1B7S; -.
PDBsum; 1BB3; -.
PDBsum; 1BB4; -.
PDBsum; 1BB5; -.
PDBsum; 1C43; -.
PDBsum; 1C45; -.
PDBsum; 1C46; -.
PDBsum; 1C7P; -.
PDBsum; 1CJ6; -.
PDBsum; 1CJ7; -.
PDBsum; 1CJ8; -.
PDBsum; 1CJ9; -.
PDBsum; 1CKC; -.
PDBsum; 1CKD; -.
PDBsum; 1CKF; -.
PDBsum; 1CKG; -.
PDBsum; 1CKH; -.
PDBsum; 1D6P; -.
PDBsum; 1D6Q; -.
PDBsum; 1DI3; -.
PDBsum; 1DI4; -.
PDBsum; 1DI5; -.
PDBsum; 1EQ4; -.
PDBsum; 1EQ5; -.
PDBsum; 1EQE; -.
PDBsum; 1GAY; -.
PDBsum; 1GAZ; -.
PDBsum; 1GB0; -.
PDBsum; 1GB2; -.
PDBsum; 1GB3; -.
PDBsum; 1GB5; -.
PDBsum; 1GB6; -.
PDBsum; 1GB7; -.
PDBsum; 1GB8; -.
PDBsum; 1GB9; -.
PDBsum; 1GBO; -.
PDBsum; 1GBW; -.
PDBsum; 1GBX; -.
PDBsum; 1GBY; -.
PDBsum; 1GBZ; -.
PDBsum; 1GDW; -.
PDBsum; 1GDX; -.
PDBsum; 1GE0; -.
PDBsum; 1GE1; -.
PDBsum; 1GE2; -.
PDBsum; 1GE3; -.
PDBsum; 1GE4; -.
PDBsum; 1GEV; -.
PDBsum; 1GEZ; -.
PDBsum; 1GF0; -.
PDBsum; 1GF3; -.
PDBsum; 1GF4; -.
PDBsum; 1GF5; -.
PDBsum; 1GF6; -.
PDBsum; 1GF7; -.
PDBsum; 1GF8; -.
PDBsum; 1GF9; -.
PDBsum; 1GFA; -.
PDBsum; 1GFE; -.
PDBsum; 1GFG; -.
PDBsum; 1GFH; -.
PDBsum; 1GFJ; -.
PDBsum; 1GFK; -.
PDBsum; 1GFR; -.
PDBsum; 1GFT; -.
PDBsum; 1GFU; -.
PDBsum; 1GFV; -.
PDBsum; 1HNL; -.
PDBsum; 1I1Z; -.
PDBsum; 1I20; -.
PDBsum; 1I22; -.
PDBsum; 1INU; -.
PDBsum; 1IOC; -.
PDBsum; 1IP1; -.
PDBsum; 1IP2; -.
PDBsum; 1IP3; -.
PDBsum; 1IP4; -.
PDBsum; 1IP5; -.
PDBsum; 1IP6; -.
PDBsum; 1IP7; -.
PDBsum; 1IWT; -.
PDBsum; 1IWU; -.
PDBsum; 1IWV; -.
PDBsum; 1IWW; -.
PDBsum; 1IWX; -.
PDBsum; 1IWY; -.
PDBsum; 1IWZ; -.
PDBsum; 1IX0; -.
PDBsum; 1IY3; -.
PDBsum; 1IY4; -.
PDBsum; 1JKA; -.
PDBsum; 1JKB; -.
PDBsum; 1JKC; -.
PDBsum; 1JKD; -.
PDBsum; 1JSF; -.
PDBsum; 1JWR; -.
PDBsum; 1LAA; -.
PDBsum; 1LHH; -.
PDBsum; 1LHI; -.
PDBsum; 1LHJ; -.
PDBsum; 1LHK; -.
PDBsum; 1LHL; -.
PDBsum; 1LHM; -.
PDBsum; 1LMT; -.
PDBsum; 1LOZ; -.
PDBsum; 1LYY; -.
PDBsum; 1LZ1; -.
PDBsum; 1LZ4; -.
PDBsum; 1LZ5; -.
PDBsum; 1LZ6; -.
PDBsum; 1LZR; -.
PDBsum; 1LZS; -.
PDBsum; 1OP9; -.
PDBsum; 1OUA; -.
PDBsum; 1OUB; -.
PDBsum; 1OUC; -.
PDBsum; 1OUD; -.
PDBsum; 1OUE; -.
PDBsum; 1OUF; -.
PDBsum; 1OUG; -.
PDBsum; 1OUH; -.
PDBsum; 1OUI; -.
PDBsum; 1OUJ; -.
PDBsum; 1QSW; -.
PDBsum; 1RE2; -.
PDBsum; 1REM; -.
PDBsum; 1REX; -.
PDBsum; 1REY; -.
PDBsum; 1REZ; -.
PDBsum; 1TAY; -.
PDBsum; 1TBY; -.
PDBsum; 1TCY; -.
PDBsum; 1TDY; -.
PDBsum; 1UBZ; -.
PDBsum; 1W08; -.
PDBsum; 1WQM; -.
PDBsum; 1WQN; -.
PDBsum; 1WQO; -.
PDBsum; 1WQP; -.
PDBsum; 1WQQ; -.
PDBsum; 1WQR; -.
PDBsum; 1YAM; -.
PDBsum; 1YAN; -.
PDBsum; 1YAO; -.
PDBsum; 1YAP; -.
PDBsum; 1YAQ; -.
PDBsum; 207L; -.
PDBsum; 208L; -.
PDBsum; 2BQA; -.
PDBsum; 2BQB; -.
PDBsum; 2BQC; -.
PDBsum; 2BQD; -.
PDBsum; 2BQE; -.
PDBsum; 2BQF; -.
PDBsum; 2BQG; -.
PDBsum; 2BQH; -.
PDBsum; 2BQI; -.
PDBsum; 2BQJ; -.
PDBsum; 2BQK; -.
PDBsum; 2BQL; -.
PDBsum; 2BQM; -.
PDBsum; 2BQN; -.
PDBsum; 2BQO; -.
PDBsum; 2HEA; -.
PDBsum; 2HEB; -.
PDBsum; 2HEC; -.
PDBsum; 2HED; -.
PDBsum; 2HEE; -.
PDBsum; 2HEF; -.
PDBsum; 2LHM; -.
PDBsum; 2MEA; -.
PDBsum; 2MEB; -.
PDBsum; 2MEC; -.
PDBsum; 2MED; -.
PDBsum; 2MEE; -.
PDBsum; 2MEF; -.
PDBsum; 2MEG; -.
PDBsum; 2MEH; -.
PDBsum; 2MEI; -.
PDBsum; 2NWD; -.
PDBsum; 2ZIJ; -.
PDBsum; 2ZIK; -.
PDBsum; 2ZIL; -.
PDBsum; 2ZWB; -.
PDBsum; 3EBA; -.
PDBsum; 3FE0; -.
PDBsum; 3LHM; -.
PDBsum; 3LN2; -.
PDBsum; 4I0C; -.
PDBsum; 4ML7; -.
PDBsum; 4R0P; -.
PDBsum; 5LSH; -.
PDBsum; 5LVK; -.
ProteinModelPortal; P61626; -.
SMR; P61626; -.
BioGrid; 110247; 35.
IntAct; P61626; 19.
MINT; P61626; -.
STRING; 9606.ENSP00000261267; -.
DrugBank; DB02159; (R)-Propylene glycol.
DrugBank; DB03175; 1-Proponol.
DrugBank; DB03487; 3-Aminosuccinimide.
DrugBank; DB02759; 4-Methylumbelliferyl Chitobiose.
DrugBank; DB03006; Arsanilic acid.
DrugBank; DB04194; Chitotriose.
DrugBank; DB02250; Cu-Bicyclam.
DrugBank; DB03189; Cu-Cyclam.
DrugBank; DB03013; Di(N-Acetyl-D-Glucosamine).
DrugBank; DB03967; Dodecyl Sulfate.
DrugBank; DB00128; L-Aspartic Acid.
DrugBank; DB04268; Methylumbelliferyl Chitotriose.
DrugBank; DB03120; Para-Toluene Sulfonate.
DrugBank; DB02772; Sucrose.
CAZy; GH22; Glycoside Hydrolase Family 22.
iPTMnet; P61626; -.
PhosphoSitePlus; P61626; -.
BioMuta; LYZ; -.
DMDM; 48428995; -.
UCD-2DPAGE; P61626; -.
EPD; P61626; -.
MaxQB; P61626; -.
PaxDb; P61626; -.
PeptideAtlas; P61626; -.
PRIDE; P61626; -.
TopDownProteomics; P61626; -.
DNASU; 4069; -.
Ensembl; ENST00000261267; ENSP00000261267; ENSG00000090382.
GeneID; 4069; -.
KEGG; hsa:4069; -.
UCSC; uc001suw.3; human.
CTD; 4069; -.
DisGeNET; 4069; -.
EuPathDB; HostDB:ENSG00000090382.6; -.
GeneCards; LYZ; -.
HGNC; HGNC:6740; LYZ.
HPA; CAB000055; -.
HPA; HPA048284; -.
MalaCards; LYZ; -.
MIM; 105200; phenotype.
MIM; 153450; gene.
neXtProt; NX_P61626; -.
OpenTargets; ENSG00000090382; -.
Orphanet; 93561; Familial renal amyloidosis due to lysozyme variant.
PharmGKB; PA30503; -.
eggNOG; ENOG410IXGD; Eukaryota.
eggNOG; ENOG4111QHM; LUCA.
GeneTree; ENSGT00550000074398; -.
HOGENOM; HOG000037357; -.
HOVERGEN; HBG052297; -.
InParanoid; P61626; -.
KO; K13915; -.
OMA; KWESNYN; -.
OrthoDB; EOG091G0R9V; -.
PhylomeDB; P61626; -.
TreeFam; TF324882; -.
BRENDA; 3.2.1.17; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6803157; Antimicrobial peptides.
Reactome; R-HSA-977225; Amyloid fiber formation.
SIGNOR; P61626; -.
ChiTaRS; LYZ; human.
EvolutionaryTrace; P61626; -.
GeneWiki; Lysozyme; -.
GenomeRNAi; 4069; -.
PRO; PR:P61626; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000090382; -.
CleanEx; HS_LYZ; -.
ExpressionAtlas; P61626; baseline and differential.
Genevisible; P61626; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003796; F:lysozyme activity; TAS:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IBA:GO_Central.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
CDD; cd00119; LYZ1; 1.
InterPro; IPR001916; Glyco_hydro_22.
InterPro; IPR019799; Glyco_hydro_22_CS.
InterPro; IPR000974; Glyco_hydro_22_lys.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR030056; Lysozyme_C.
PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
Pfam; PF00062; Lys; 1.
PRINTS; PR00137; LYSOZYME.
PRINTS; PR00135; LYZLACT.
SMART; SM00263; LYZ1; 1.
SUPFAM; SSF53955; SSF53955; 1.
PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1.
PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
1: Evidence at protein level;
3D-structure; Amyloid; Amyloidosis; Antimicrobial;
Bacteriolytic enzyme; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycosidase; Hydrolase;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:11946553,
ECO:0000269|PubMed:11946554,
ECO:0000269|PubMed:25946035,
ECO:0000269|PubMed:5168859,
ECO:0000269|PubMed:5284421}.
CHAIN 19 148 Lysozyme C.
/FTId=PRO_0000018467.
ACT_SITE 53 53
ACT_SITE 71 71
DISULFID 24 146
DISULFID 48 134
DISULFID 83 99
DISULFID 95 113
VARIANT 74 74 I -> T (in AMYL8; dbSNP:rs121913547).
{ECO:0000269|PubMed:8464497}.
/FTId=VAR_004280.
VARIANT 85 85 D -> H (in AMYL8; dbSNP:rs121913548).
{ECO:0000269|PubMed:8464497}.
/FTId=VAR_004281.
VARIANT 88 88 T -> N (in dbSNP:rs1800973).
/FTId=VAR_012050.
CONFLICT 10 10 V -> A (in Ref. 5; AAC63078).
{ECO:0000305}.
CONFLICT 41 41 I -> M (in Ref. 1; AAA36188).
{ECO:0000305}.
CONFLICT 111 111 V -> A (in Ref. 5; AAC63078).
{ECO:0000305}.
CONFLICT 124 124 I -> V (in Ref. 5; AAC63078).
{ECO:0000305}.
CONFLICT 128 128 V -> A (in Ref. 5; AAC63078).
{ECO:0000305}.
CONFLICT 136 136 N -> D (in Ref. 5; AAC63078).
{ECO:0000305}.
HELIX 23 32 {ECO:0000244|PDB:2NWD}.
HELIX 38 40 {ECO:0000244|PDB:1BB3}.
HELIX 43 54 {ECO:0000244|PDB:2NWD}.
STRAND 55 57 {ECO:0000244|PDB:2NWD}.
STRAND 61 63 {ECO:0000244|PDB:2NWD}.
TURN 65 67 {ECO:0000244|PDB:2NWD}.
STRAND 70 72 {ECO:0000244|PDB:2NWD}.
TURN 73 76 {ECO:0000244|PDB:2NWD}.
TURN 79 81 {ECO:0000244|PDB:2NWD}.
STRAND 82 84 {ECO:0000244|PDB:2NWD}.
STRAND 88 90 {ECO:0000244|PDB:1LHI}.
HELIX 99 103 {ECO:0000244|PDB:2NWD}.
STRAND 104 106 {ECO:0000244|PDB:2NWD}.
HELIX 108 119 {ECO:0000244|PDB:2NWD}.
STRAND 120 122 {ECO:0000244|PDB:1B7M}.
HELIX 123 126 {ECO:0000244|PDB:2NWD}.
HELIX 128 133 {ECO:0000244|PDB:2NWD}.
TURN 134 136 {ECO:0000244|PDB:2NWD}.
HELIX 140 142 {ECO:0000244|PDB:2NWD}.
TURN 143 145 {ECO:0000244|PDB:2NWD}.
SEQUENCE 148 AA; 16537 MW; 8ECFD276BEB2678A CRC64;
MKALIVLGLV LLSVTVQGKV FERCELARTL KRLGMDGYRG ISLANWMCLA KWESGYNTRA
TNYNAGDRST DYGIFQINSR YWCNDGKTPG AVNACHLSCS ALLQDNIADA VACAKRVVRD
PQGIRAWVAW RNRCQNRDVR QYVQGCGV


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