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

Chondroitin sulfate ABC exolyase (EC 4.2.2.21) (Chondroitin ABC exoeliminase) (Chondroitin ABC lyase II) (Chondroitin sulfate ABC lyase II) (ChS ABC lyase II) (Chondroitinase ABC II) (cABC II) (Exochondroitinase ABC) (Fragment)

 CABC2_PROVU             Reviewed;         990 AA.
C7S340;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
13-OCT-2009, sequence version 1.
18-JUL-2018, entry version 26.
RecName: Full=Chondroitin sulfate ABC exolyase;
EC=4.2.2.21;
AltName: Full=Chondroitin ABC exoeliminase;
AltName: Full=Chondroitin ABC lyase II;
AltName: Full=Chondroitin sulfate ABC lyase II;
Short=ChS ABC lyase II;
AltName: Full=Chondroitinase ABC II;
Short=cABC II;
AltName: Full=Exochondroitinase ABC;
Flags: Fragment;
Name=ChABCII;
Proteus vulgaris.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Morganellaceae; Proteus.
NCBI_TaxID=585;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
Tam K.-W., Wang Q., Li R.A., Chan Y.-S., Shum D.K.-Y.;
"Cloning, recombinant expression, characterization and mutagenesis of
chondroitin sulphate ABC exolyase from Proteus vulgaris.";
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME
REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
PubMed=9083041; DOI=10.1074/jbc.272.14.9123;
Hamai A., Hashimoto N., Mochizuki H., Kato F., Makiguchi Y., Horie K.,
Suzuki S.;
"Two distinct chondroitin sulfate ABC lyases. An endoeliminase
yielding tetrasaccharides and an exoeliminase preferentially acting on
oligosaccharides.";
J. Biol. Chem. 272:9123-9130(1997).
[3]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE RESIDUES, AND MUTAGENESIS
OF HIS-343; HIS-452; HIS-453; HIS-456; TYR-460; ARG-513 AND GLU-608.
STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
PubMed=18849565; DOI=10.1074/jbc.M806630200;
Prabhakar V., Capila I., Soundararajan V., Raman R., Sasisekharan R.;
"Recombinant expression, purification, and biochemical
characterization of chondroitinase ABC II from Proteus vulgaris.";
J. Biol. Chem. 284:974-982(2009).
-!- FUNCTION: Broad-specificity glycosaminoglycan lyase, which acts in
an exolytic fashion, and preferentially degrades the tetra- and
hexasaccharide derivatives of chondroitin sulfate and dermatan
sulfate produced by the chondroitin sulfate ABC endolyase, to
yield the respective disaccharides. To a lesser extent, is also
able to split off disaccharide residues directly from polymeric
chondroitin 4- and 6-sulfate, dermatan sulfate, chondroitin, and
hyaluronan. Is not active against keratan sulfate, heparan
sulfate, and heparin. {ECO:0000269|PubMed:18849565,
ECO:0000269|PubMed:9083041}.
-!- CATALYTIC ACTIVITY: Exolytic removal of Delta(4)-unsaturated
disaccharide residues from the non-reducing ends of both polymeric
chondroitin/dermatan sulfates and their oligosaccharide fragments.
{ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}.
-!- ENZYME REGULATION: Inhibited by Zn(2+), whereas Ni(2+), Fe(2+),
and Cu(2+) have little or no effect on activity.
{ECO:0000269|PubMed:9083041}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=33 uM for chondroitin 6-sulfate tetrasaccharide
{ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
KM=80 uM for chondroitin 6-sulfate {ECO:0000269|PubMed:18849565,
ECO:0000269|PubMed:9083041};
KM=9.8 uM for chondroitin 6-sulfate
{ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
KM=16.1 uM for chondroitin 4-sulfate
{ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
KM=19.2 uM for dermatan sulfate {ECO:0000269|PubMed:18849565,
ECO:0000269|PubMed:9083041};
Vmax=155 umol/min/mg enzyme with chondroitin 6-sulfate
tetrasaccharide as substrate {ECO:0000269|PubMed:18849565,
ECO:0000269|PubMed:9083041};
Vmax=34 umol/min/mg enzyme with chondroitin 6-sulfate as
substrate {ECO:0000269|PubMed:18849565,
ECO:0000269|PubMed:9083041};
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:18849565,
ECO:0000269|PubMed:9083041};
Temperature dependence:
Optimum temperature is 40 degrees Celsius (PubMed:9083041).
Optimum temperature is 37 degrees Celsius (PubMed:18849565).
{ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
-!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; EF988659; ABU46331.1; -; Genomic_DNA.
SMR; C7S340; -.
BioCyc; MetaCyc:MONOMER-15789; -.
GO; GO:0005576; C:extracellular region; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0034000; F:chondroitin-sulfate-ABC endolyase activity; IEA:InterPro.
GO; GO:0034001; F:chondroitin-sulfate-ABC exolyase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
Gene3D; 1.50.10.100; -; 1.
Gene3D; 2.60.220.10; -; 1.
Gene3D; 2.70.98.10; -; 1.
InterPro; IPR039174; Chondroitin_ABC_lyase.
InterPro; IPR008929; Chondroitin_lyas.
InterPro; IPR024200; Chondroitinase_ABC_I.
InterPro; IPR011013; Gal_mutarotase_sf_dom.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR014718; GH-type_carb-bd.
InterPro; IPR011071; Lyase_8-like_C.
InterPro; IPR004103; Lyase_8_C.
InterPro; IPR003159; Lyase_8_central_dom.
InterPro; IPR015177; Lyase_catalyt.
InterPro; IPR015176; Lyase_N.
PANTHER; PTHR37322; PTHR37322; 1.
Pfam; PF02278; Lyase_8; 1.
Pfam; PF02884; Lyase_8_C; 1.
Pfam; PF09093; Lyase_catalyt; 1.
Pfam; PF09092; Lyase_N; 1.
PIRSF; PIRSF034515; Chondroitinase; 1.
SUPFAM; SSF48230; SSF48230; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF49863; SSF49863; 1.
SUPFAM; SSF74650; SSF74650; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Lyase.
CHAIN <1 990 Chondroitin sulfate ABC exolyase.
/FTId=PRO_0000413627.
ACT_SITE 453 453 Proton acceptor.
{ECO:0000305|PubMed:18849565}.
ACT_SITE 460 460 Proton donor. {ECO:0000255}.
SITE 513 513 Transition state stabilizer.
{ECO:0000255}.
SITE 608 608 Important for catalytic activity.
MUTAGEN 343 343 H->A: Loss of activity on both
chondroitin 6-sulfate and dermatan
sulfate. {ECO:0000269|PubMed:18849565}.
MUTAGEN 452 452 H->A: Slight decrease in substrate
affinity, but greatly reduced (100-fold)
catalytic efficiency.
{ECO:0000269|PubMed:18849565}.
MUTAGEN 453 453 H->A: Loss of activity on both
chondroitin 6-sulfate and dermatan
sulfate. {ECO:0000269|PubMed:18849565}.
MUTAGEN 456 456 H->A: 3-fold decrease in catalytic
efficiency with both chondroitin 6-
sulfate and dermatan sulfate.
{ECO:0000269|PubMed:18849565}.
MUTAGEN 460 460 Y->A: Loss of activity on both
chondroitin 6-sulfate and dermatan
sulfate. {ECO:0000269|PubMed:18849565}.
MUTAGEN 513 513 R->A: Loss of activity on both
chondroitin 6-sulfate and dermatan
sulfate. {ECO:0000269|PubMed:18849565}.
MUTAGEN 608 608 E->A: Loss of activity on both
chondroitin 6-sulfate and dermatan
sulfate. {ECO:0000269|PubMed:18849565}.
NON_TER 1 1
SEQUENCE 990 AA; 111744 MW; 7AA786306AAADF08 CRC64;
LPTLSHEAFG DIYLFEGELP NTLTTSNNNQ LSLSKQHAKD GEQSLKWQYQ PQATLTLNNI
VNYQDDKNTA TPLTFMMWIY NEKPQSSPLT LAFKQNNKIA LSFNAELNFT GWRGIAVPFR
DMQGSATGQL DQLVITAPNQ AGTLFFDQII MSVPLDNRWA VPDYQTPYVN NAVNTMVSKN
WSALLMYDQM FQAHYPTLNF DTEFRDDQTE MASIYQRFEY YQGIRSDKKI TPDMLDKHLA
LWEKLVLTQH ADGSITGKAL DHPNRQHFMK VEGVFSEGTQ KALLDANMLR DVGKTLLQTA
IYLRSDSLSA TDRKKLEERY LLGTRYVLEQ GFTRGSGYQI ITHVGYQTRE LFDAWFIGRH
VLAKNNLLAP TQQAMMWYNA TGRIFEKNNE IVDANVDILN TQLQWMIKSL LMLPDYQQRQ
QALAQLQSWL NKTILSSKGV AGGFKSDGSI FHHSQHYPAY AKDAFGGLAP SVYALSDSPF
RLSTSAHERL KDVLLKMRIY TKETQIPVVL SGRHPTGLHK IGIAPFKWMA LAGTPDGKQK
LDTTLSAAYA KLDNKTHFEG INAESEPVGA WAMNYASMAI QRRASTQSPQ QSWLAIARGF
SRYLVGNESY ENNNRYGRYL QYGQLEIIPA DLTQSGFSHA GWDWNRYPGT TTIHLPYNEL
EAKLNQLPAA GIEEMLLSTE SYSGANTLNN NSMFAMKLHG HSKYQQQSLR ANKSYFLFDN
RVIALGSGIE NDDKQHTTET TLFQFAVPKL QSVIINGKKV NQLDTQLTLN NADTLIDPTG
NLYKLTKGQT VKFSYQKQHS LDDRNSKPTE QLFATAVISH GKAPSNENYE YAIAIEAQNN
KAPEYTVLQH NDQLHAVKDK ITQEEGYAFF EATKLKSADA TLLSSDAPVM VMAKIQNQQL
TLSIVNPDLN LYQGREKDQF DDKGNQIEVS VYSRHWLTAE SQSTNSTITV KGIWKLTTPQ
PGVIIKHHNN NTLITTTTIQ ATPTVINLVK


Related products :

Catalog number Product name Quantity
EIAAB07242 Chondroitin glucuronyltransferase,Chondroitin polymerizing factor 2,Chondroitin sulfate glucuronyltransferase,Chondroitin synthase 3,CHPF2,ChPF-2,CHSY3,ChSy-3,CSGLCAT,CSGlcA-T,Homo sapiens,Human,KIAA1
EIAAB09627 Chondroitin sulfate proteoglycan 4,Chondroitin sulfate proteoglycan NG2,CSPG4,Homo sapiens,Human,MCSP,Melanoma chondroitin sulfate proteoglycan,Melanoma-associated chondroitin sulfate proteoglycan
EIAAB07263 Chondroitin glucuronyltransferase 1,Chondroitin sulfate synthase 1,Chondroitin synthase 1,Chsy1,ChSy-1,Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase 1,Kiaa0
EIAAB07264 Chondroitin glucuronyltransferase 2,Chondroitin sulfate synthase 2,Chondroitin-polymerizing factor,ChPF,CHPF,CSS2,Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransfer
EIAAB07265 Chondroitin glucuronyltransferase 2,Chondroitin sulfate synthase 2,Chondroitin-polymerizing factor,ChPF,Chpf,Css2,D1Bwg1363e,Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosami
EIAAB07266 Carbohydrate synthase 2,Chondroitin glucuronyltransferase 3,Chondroitin sulfate synthase 3,Chondroitin synthase 2,Chsy2,ChSy-2,Chsy3,Css3,Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acet
EIAAB07267 Carbohydrate synthase 2,Chondroitin glucuronyltransferase 3,Chondroitin sulfate synthase 3,Chondroitin synthase 2,CHSY2,ChSy-2,CHSY3,CSS3,Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acet
30-500 CHST13 catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage a 0.05 mg
26-376 CHST13 catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage a 0.05 mg
30-501 CHST13 catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage a 0.05 mg
EIAAB07262 Chondroitin glucuronyltransferase 1,Chondroitin sulfate synthase 1,Chondroitin synthase 1,CHSY,CHSY1,ChSy-1,CSS1,Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransfera
9082-07-9 Chondroitin sulfate sodium salt Chondroitin sulfate sodi 1g
EIAAB09629 Chondroitin sulfate proteoglycan 4,Chondroitin sulfate proteoglycan NG2,Cspg4,HSN tumor-specific antigen,Ng2,Rat,Rattus norvegicus
86016-46-8 Chondroitin sulfate calcium salt Chondroitin sulfate Cal 1g
12678-07-8 Chondroitin sulfate C sodium salt Chondroitin sulfate C S 1g
U1817r CLIA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan, 96T
E1817r ELISA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan 96T
E1817b ELISA kit Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Ver 96T
E1817b ELISA Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Versican 96T
U1817h CLIA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Homo sapiens,Human,Large fibroblast proteoglycan,PG-M,VCAN,Ver 96T
E1817h ELISA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Homo sapiens,Human,Large fibroblast proteoglycan,PG-M,VCAN,Ve 96T
U1817b CLIA kit Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Vers 96T
U1817b CLIA Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Versican 96T
U1817r CLIA Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan,Versi 96T
E1817r ELISA Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan,Vers 96T


 

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