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

Chlorite dismutase (EC 1.13.11.49) (Chlorite O(2)-lyase)

 CLD_IDEDE               Reviewed;         285 AA.
Q9F437;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 35.
RecName: Full=Chlorite dismutase;
EC=1.13.11.49;
AltName: Full=Chlorite O(2)-lyase;
Flags: Precursor;
Name=cld;
Ideonella dechloratans.
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Ideonella.
NCBI_TaxID=36863;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-63; 77-87
AND 171-185, AND COFACTOR.
STRAIN=ATCC 51718 / CCUG 30977;
PubMed=12359335; DOI=10.1016/S0167-4781(02)00446-3;
Danielsson Thorell H., Karlsson J., Portelius E., Nilsson T.;
"Cloning, characterisation, and expression of a novel gene encoding
chlorite dismutase from Ideonella dechloratans.";
Biochim. Biophys. Acta 1577:445-451(2002).
[2]
PROTEIN SEQUENCE OF 39-60, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 51718 / CCUG 30977;
PubMed=11472023; DOI=10.1007/s007750100237;
Stenklo K., Danielsson Thorell H., Bergius H., Aasa R., Nilsson T.;
"Chlorite dismutase from Ideonella dechloratans.";
J. Biol. Inorg. Chem. 6:601-607(2001).
[3]
PROTEIN SEQUENCE OF 281-285, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=ATCC 51718 / CCUG 30977;
PubMed=15317589; DOI=10.1111/j.0014-2956.2004.04290.x;
Danielsson Thorell H., Beyer N.H., Heegaard N.H., Oehman M.,
Nilsson T.;
"Comparison of native and recombinant chlorite dismutase from
Ideonella dechloratans.";
Eur. J. Biochem. 271:3539-3546(2004).
[4]
FUNCTION, AND INDUCTION.
STRAIN=ATCC 51718 / CCUG 30977;
PubMed=22492460; DOI=10.1128/AEM.07303-11;
Lindqvist M.H., Johansson N., Nilsson T., Rova M.;
"Expression of chlorite dismutase and chlorate reductase in the
presence of oxygen and/or chlorate as the terminal electron acceptor
in Ideonella dechloratans.";
Appl. Environ. Microbiol. 78:4380-4385(2012).
-!- FUNCTION: Catalyzes the heme-dependent decomposition of chlorite
to O(2) and chloride with high efficiency and specificity. Used to
detoxify chlorite, a by-product of the reduction of perchlorate, a
primarily anthropogenic pollutant, in perchlorate-respiring
bacteria. {ECO:0000269|PubMed:11472023,
ECO:0000269|PubMed:22492460}.
-!- CATALYTIC ACTIVITY: Chloride + O(2) = chlorite.
{ECO:0000269|PubMed:11472023}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:11472023,
ECO:0000269|PubMed:12359335};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
monomer. {ECO:0000269|PubMed:11472023,
ECO:0000269|PubMed:12359335};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.26 mM for chlorite {ECO:0000269|PubMed:11472023};
Vmax=4.3 mmol/min/mg enzyme {ECO:0000269|PubMed:11472023};
-!- SUBUNIT: Homopentamer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11472023}.
-!- INDUCTION: Expressed under aerobic conditions. Significantly
increased upon shift to anaerobic conditions.
{ECO:0000269|PubMed:22492460}.
-!- SIMILARITY: Belongs to the chlorite dismutase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ296077; CAC14884.1; -; Genomic_DNA.
ProteinModelPortal; Q9F437; -.
SMR; Q9F437; -.
KEGG; ag:CAC14884; -.
KO; K09162; -.
GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
GO; GO:0050587; F:chlorite O2-lyase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
InterPro; IPR011008; Dimeric_a/b-barrel.
InterPro; IPR010644; Put_peroxidase/dismutase.
PANTHER; PTHR36843; PTHR36843; 1.
Pfam; PF06778; Chlor_dismutase; 1.
SUPFAM; SSF54909; SSF54909; 1.
1: Evidence at protein level;
Calcium; Direct protein sequencing; Heme; Iron; Metal-binding;
Oxidoreductase; Periplasm; Signal.
SIGNAL 1 38 {ECO:0000269|PubMed:11472023,
ECO:0000269|PubMed:12359335}.
CHAIN 39 285 Chlorite dismutase.
/FTId=PRO_5000066624.
ACT_SITE 218 218 Proton acceptor. {ECO:0000250}.
METAL 105 105 Calcium. {ECO:0000250}.
METAL 205 205 Iron (heme axial ligand); via tele
nitrogen. {ECO:0000250}.
METAL 227 227 Calcium. {ECO:0000250}.
METAL 266 266 Calcium; via carbonyl oxygen.
{ECO:0000250}.
CONFLICT 59 59 F -> P (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 285 AA; 31429 MW; BE83EA65AB19D9D0 CRC64;
MKVRCVSLVA AGLLTIAGSA IGQPAPAPMP AMAPAAKPAM NTPVDRAKIL SAPGVFVAFS
TYKIRPDYFK VALAERKGAA DEVMAVLEKH KEKVIVDAYL TRGYEAKSDY FLRVHAYDAV
AAQAFLVDFR ATRFGMYSDV TESLVGITKA LNYISKDKSP DLNKGLSGAT YAGDAPRFAF
MIPVKKNADW WNLTDEQRLK EMETHTLPTL PFLVNVKRKL YHSTGLDDTD FITYFETNDL
GAFNNLMLSL AKVPENKYHV RWGNPTVLGT IQPIENLVKT LSMGN


Related products :

Catalog number Product name Quantity
S04524 Sodium chlorite Tech. Grade 500 G
S04524 Sodium chlorite Tech. Grade 100 G
S04524 Sodium chlorite Tech. Grade 1000 G
S04524 Sodium chlorite Tech. Grade 500 G
S04524 Sodium chlorite Tech. Grade 100 G
S04524 Sodium chlorite Tech. Grade 1000 G
S04524 Sodium chlorite solution Tech. Grade 100 G
S04524 Sodium chlorite solution Tech. Grade 1000 G
S04524 Sodium chlorite solution Tech. Grade 500 G
0582301000 SODIUM CHLORITE FLAKES CRYSTALS 80 percent , CAS: 7758-19-2 2x1KGS
0582300250 SODIUM CHLORITE FLAKES _ CRYSTALS 80 percent , CAS: 7758-19-2 5x250GM
0582301000 SODIUM CHLORITE FLAKES _ CRYSTALS 80 percent , CAS: 7758-19-2 2x1KGS
0582300250 SODIUM CHLORITE FLAKES CRYSTALS 80 percent , CAS: 7758-19-2 5x250GM
EIAAB27670 Mouse,Mus musculus,N-acetylneuraminate lyase,N-acetylneuraminate pyruvate-lyase,N-acetylneuraminic acid aldolase,NALase,Npl,Sialate lyase,Sialate-pyruvate lyase,Sialic acid aldolase,Sialic acid lyase
EIAAB27668 Bos taurus,Bovine,N-acetylneuraminate lyase,N-acetylneuraminate pyruvate-lyase,N-acetylneuraminic acid aldolase,NALase,NPL,Sialate lyase,Sialate-pyruvate lyase,Sialic acid aldolase,Sialic acid lyase
EIAAB27669 N-acetylneuraminate lyase,N-acetylneuraminate pyruvate-lyase,N-acetylneuraminic acid aldolase,NALase,NPL,Pig,Sialate lyase,Sialate-pyruvate lyase,Sialic acid aldolase,Sialic acid lyase,Sus scrofa
EIAAB27666 C1orf13,Homo sapiens,Human,N-acetylneuraminate lyase,N-acetylneuraminate pyruvate-lyase,N-acetylneuraminic acid aldolase,NALase,NPL,Sialate lyase,Sialate-pyruvate lyase,Sialic acid aldolase,Sialic aci
EIAAB27665 Chicken,Gallus gallus,N-acetylneuraminate lyase,N-acetylneuraminate pyruvate-lyase,N-acetylneuraminic acid aldolase,NALase,NPL,RCJMB04_11j23,Sialate lyase,Sialate-pyruvate lyase,Sialic acid aldolase,S
EIAAB27667 N-acetylneuraminate lyase,N-acetylneuraminate pyruvate-lyase,N-acetylneuraminic acid aldolase,NALase,Npl,Rat,Rattus norvegicus,Sialate lyase,Sialate-pyruvate lyase,Sialic acid aldolase,Sialic acid lya
ESOD-100 EnzyChrom™ Superoxide Dismutase Assay Kit, Quantitative determination of superoxide dismutase (SOD) enzyme activity by colorimetric (440nm) method 100Tests
U0596h CLIA Homo sapiens,hSod1,Human,SOD1,Superoxide dismutase [Cu-Zn],Superoxide dismutase 1 96T
E0596h ELISA kit Homo sapiens,hSod1,Human,SOD1,Superoxide dismutase [Cu-Zn],Superoxide dismutase 1 96T
E0596h ELISA Homo sapiens,hSod1,Human,SOD1,Superoxide dismutase [Cu-Zn],Superoxide dismutase 1 96T
EIAAB38151 Homo sapiens,hSPL,Human,KIAA1252,S1PL,SGPL1,Sphingosine-1-phosphate aldolase,Sphingosine-1-phosphate lyase 1,SPL 1,SP-lyase 1
EIAAB08028 Citrate lyase beta-like,Citrate lyase subunit beta-like protein, mitochondrial,CLB,CLYBL,Homo sapiens,Human


 

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