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

Arylsulfatase (AS) (EC 3.1.6.1) (Aryl-sulfate sulphohydrolase)

 ARS_PSEAE               Reviewed;         536 AA.
P51691;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 130.
RecName: Full=Arylsulfatase;
Short=AS;
EC=3.1.6.1 {ECO:0000269|PubMed:7744061, ECO:0000269|PubMed:9748219};
AltName: Full=Aryl-sulfate sulphohydrolase;
Name=atsA; OrderedLocusNames=PA0183;
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=208964;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
AND CATALYTIC ACTIVITY.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=7744061; DOI=10.1111/j.1432-1033.1995.0385k.x;
Beil S., Kehrli H., James P., Staudenmann W., Cook A.M., Leisinger T.,
Kertesz M.A.;
"Purification and characterization of the arylsulfatase synthesized by
Pseudomonas aeruginosa PAO during growth in sulfate-free medium and
cloning of the arylsulfatase gene (atsA).";
Eur. J. Biochem. 229:385-394(1995).
[2]
SEQUENCE REVISION.
Kertesz M.A.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=10984043; DOI=10.1038/35023079;
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an
opportunistic pathogen.";
Nature 406:959-964(2000).
[4]
FUNCTION, CATALYTIC ACTIVITY, OXOALANINE AT CYS-51, AND MUTAGENESIS OF
CYS-51.
PubMed=9748219;
Dierks T., Miech C., Hummerjohann J., Schmidt B., Kertesz M.A.,
von Figura K.;
"Posttranslational formation of formylglycine in prokaryotic
sulfatases by modification of either cysteine or serine.";
J. Biol. Chem. 273:25560-25564(1998).
[5]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), AND OXOALANINE AT CYS-51.
PubMed=11435113; DOI=10.1016/S0969-2126(01)00609-8;
Boltes I., Czapinska H., Kahnert A., von Buelow R., Dierks T.,
Schmidt B., von Figura K., Kertesz M.A., Uson I.;
"1.3 A structure of arylsulfatase from Pseudomonas aeruginosa
establishes the catalytic mechanism of sulfate ester cleavage in the
sulfatase family.";
Structure 9:483-491(2001).
-!- FUNCTION: Hydrolyzes the bond between sulfate and the aromatic
ring in a compound such as 4-nitrocatechol sulfate.
{ECO:0000269|PubMed:7744061, ECO:0000269|PubMed:9748219}.
-!- CATALYTIC ACTIVITY: A phenol sulfate + H(2)O = a phenol + sulfate.
{ECO:0000269|PubMed:7744061, ECO:0000269|PubMed:9748219}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:11435113};
Note=Binds 1 Ca(2+) ion per subunit.
{ECO:0000269|PubMed:11435113};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.9.;
Temperature dependence:
Optimum temperature is 57 degrees Celsius. Incubation that
exceeds 20 minutes above 50 degrees Celsius leads to enzyme
inactivation.;
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- PTM: The conversion to 3-oxoalanine (also known as C-
formylglycine, FGly), of a serine or cysteine residue in
prokaryotes and of a cysteine residue in eukaryotes, is critical
for catalytic activity. {ECO:0000269|PubMed:11435113,
ECO:0000269|PubMed:9748219}.
-!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z48540; CAA88421.2; -; Genomic_DNA.
EMBL; AE004091; AAG03573.1; -; Genomic_DNA.
PIR; D83622; D83622.
PIR; S69336; S69336.
RefSeq; NP_248873.1; NC_002516.2.
RefSeq; WP_003106692.1; NC_002516.2.
PDB; 1HDH; X-ray; 1.30 A; A/B=1-536.
PDB; 4CXK; X-ray; 1.86 A; A/B=1-534.
PDB; 4CXS; X-ray; 2.30 A; A/B=1-536.
PDB; 4CXU; X-ray; 2.03 A; A/B=1-536.
PDB; 4CYR; X-ray; 1.72 A; A/B=1-536.
PDB; 4CYS; X-ray; 1.88 A; A/B=1-536.
PDB; 5AJ9; X-ray; 2.00 A; A/B=1-536.
PDBsum; 1HDH; -.
PDBsum; 4CXK; -.
PDBsum; 4CXS; -.
PDBsum; 4CXU; -.
PDBsum; 4CYR; -.
PDBsum; 4CYS; -.
PDBsum; 5AJ9; -.
ProteinModelPortal; P51691; -.
SMR; P51691; -.
STRING; 208964.PA0183; -.
BindingDB; P51691; -.
ChEMBL; CHEMBL5816; -.
DrugBank; DB02289; 2-Aminopropanedioic Acid.
PaxDb; P51691; -.
EnsemblBacteria; AAG03573; AAG03573; PA0183.
GeneID; 879288; -.
KEGG; pae:PA0183; -.
PATRIC; fig|208964.12.peg.189; -.
PseudoCAP; PA0183; -.
eggNOG; ENOG4107QRH; Bacteria.
eggNOG; COG3119; LUCA.
HOGENOM; HOG000135353; -.
InParanoid; P51691; -.
KO; K01130; -.
OMA; QMPENAW; -.
PhylomeDB; P51691; -.
BioCyc; PAER208964:G1FZ6-184-MONOMER; -.
BRENDA; 3.1.6.1; 5087.
EvolutionaryTrace; P51691; -.
PRO; PR:P51691; -.
Proteomes; UP000002438; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004065; F:arylsulfatase activity; IDA:PseudoCAP.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:PseudoCAP.
GO; GO:0008152; P:metabolic process; IEA:InterPro.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR024607; Sulfatase_CS.
InterPro; IPR000917; Sulfatase_N.
Pfam; PF00884; Sulfatase; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00523; SULFATASE_1; 1.
PROSITE; PS00149; SULFATASE_2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Metal-binding;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7744061}.
CHAIN 2 536 Arylsulfatase.
/FTId=PRO_0000192683.
ACT_SITE 51 51 Nucleophile.
{ECO:0000269|PubMed:11435113,
ECO:0000269|PubMed:9748219}.
ACT_SITE 115 115 {ECO:0000250|UniProtKB:P15289}.
METAL 13 13 Calcium. {ECO:0000269|PubMed:11435113}.
METAL 14 14 Calcium. {ECO:0000269|PubMed:11435113}.
METAL 51 51 Calcium; via 3-oxoalanine.
{ECO:0000269|PubMed:11435113}.
METAL 317 317 Calcium. {ECO:0000269|PubMed:11435113}.
METAL 318 318 Calcium. {ECO:0000269|PubMed:11435113}.
MOD_RES 51 51 3-oxoalanine (Cys).
{ECO:0000269|PubMed:11435113,
ECO:0000269|PubMed:9748219}.
MUTAGEN 51 51 C->S: Abolishes formation of 3-oxoalanine
(also known as C-formylglycine, FGly).
Strongly reduced enzyme activity.
{ECO:0000269|PubMed:9748219}.
CONFLICT 2 2 S -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
STRAND 6 14 {ECO:0000244|PDB:1HDH}.
HELIX 21 23 {ECO:0000244|PDB:1HDH}.
HELIX 30 38 {ECO:0000244|PDB:1HDH}.
STRAND 39 46 {ECO:0000244|PDB:1HDH}.
HELIX 51 58 {ECO:0000244|PDB:1HDH}.
HELIX 64 67 {ECO:0000244|PDB:1HDH}.
HELIX 73 75 {ECO:0000244|PDB:1HDH}.
TURN 78 82 {ECO:0000244|PDB:1HDH}.
STRAND 87 89 {ECO:0000244|PDB:1HDH}.
STRAND 92 94 {ECO:0000244|PDB:1HDH}.
HELIX 97 102 {ECO:0000244|PDB:1HDH}.
TURN 103 105 {ECO:0000244|PDB:1HDH}.
STRAND 107 113 {ECO:0000244|PDB:1HDH}.
HELIX 120 122 {ECO:0000244|PDB:1HDH}.
TURN 124 128 {ECO:0000244|PDB:1HDH}.
STRAND 130 135 {ECO:0000244|PDB:1HDH}.
HELIX 155 158 {ECO:0000244|PDB:1HDH}.
STRAND 164 166 {ECO:0000244|PDB:1HDH}.
HELIX 180 193 {ECO:0000244|PDB:1HDH}.
STRAND 201 206 {ECO:0000244|PDB:1HDH}.
STRAND 211 213 {ECO:0000244|PDB:1HDH}.
HELIX 218 221 {ECO:0000244|PDB:1HDH}.
HELIX 222 224 {ECO:0000244|PDB:1HDH}.
TURN 225 230 {ECO:0000244|PDB:1HDH}.
HELIX 231 245 {ECO:0000244|PDB:1HDH}.
HELIX 265 267 {ECO:0000244|PDB:1HDH}.
HELIX 270 303 {ECO:0000244|PDB:1HDH}.
HELIX 307 309 {ECO:0000244|PDB:1HDH}.
STRAND 310 319 {ECO:0000244|PDB:1HDH}.
HELIX 325 327 {ECO:0000244|PDB:1HDH}.
HELIX 329 331 {ECO:0000244|PDB:1HDH}.
HELIX 335 342 {ECO:0000244|PDB:1HDH}.
HELIX 347 349 {ECO:0000244|PDB:1HDH}.
HELIX 360 368 {ECO:0000244|PDB:1HDH}.
STRAND 371 373 {ECO:0000244|PDB:1HDH}.
STRAND 377 379 {ECO:0000244|PDB:1HDH}.
HELIX 380 383 {ECO:0000244|PDB:1HDH}.
STRAND 387 390 {ECO:0000244|PDB:1HDH}.
STRAND 398 401 {ECO:0000244|PDB:1HDH}.
HELIX 407 409 {ECO:0000244|PDB:1HDH}.
HELIX 410 418 {ECO:0000244|PDB:1HDH}.
STRAND 425 427 {ECO:0000244|PDB:1HDH}.
HELIX 441 444 {ECO:0000244|PDB:1HDH}.
STRAND 447 449 {ECO:0000244|PDB:1HDH}.
STRAND 457 462 {ECO:0000244|PDB:1HDH}.
STRAND 465 470 {ECO:0000244|PDB:1HDH}.
STRAND 473 477 {ECO:0000244|PDB:1HDH}.
TURN 480 482 {ECO:0000244|PDB:1HDH}.
STRAND 485 491 {ECO:0000244|PDB:1HDH}.
TURN 492 494 {ECO:0000244|PDB:1HDH}.
TURN 503 505 {ECO:0000244|PDB:1HDH}.
HELIX 507 524 {ECO:0000244|PDB:1HDH}.
SEQUENCE 536 AA; 59946 MW; E926EC099E14EA63 CRC64;
MSKRPNFLVI VADDLGFSDI GAFGGEIATP NLDALAIAGL RLTDFHTAST CSPTRSMLLT
GTDHHIAGIG TMAEALTPEL EGKPGYEGHL NERVVALPEL LREAGYQTLM AGKWHLGLKP
EQTPHARGFE RSFSLLPGAA NHYGFEPPYD ESTPRILKGT PALYVEDERY LDTLPEGFYS
SDAFGDKLLQ YLKERDQSRP FFAYLPFSAP HWPLQAPREI VEKYRGRYDA GPEALRQERL
ARLKELGLVE ADVEAHPVLA LTREWEALED EERAKSARAM EVYAAMVERM DWNIGRVVDY
LRRQGELDNT FVLFMSDNGA EGALLEAFPK FGPDLLGFLD RHYDNSLENI GRANSYVWYG
PRWAQAATAP SRLYKAFTTQ GGIRVPALVR YPRLSRQGAI SHAFATVMDV TPTLLDLAGV
RHPGKRWRGR EIAEPRGRSW LGWLSGETEA AHDENTVTGW ELFGMRAIRQ GDWKAVYLPA
PVGPATWQLY DLARDPGEIH DLADSQPGKL AELIEHWKRY VSETGVVEGA SPFLVR


Related products :

Catalog number Product name Quantity
M1388 4-Methylumbelliferyl sulfate, potassium salt, Highly sensitive fluorescent substrate for monitoring aryl sulfatase activity, 25mg
M1388 4_Methylumbelliferyl sulfate, potassium salt, Highly sensitive fluorescent substrate for monitoring aryl sulfatase activity, 25mg
CA15 N-Sulphoglucosamine Sulphohydrolase SGSH 500
CA15 N-Sulphoglucosamine Sulphohydrolase SGSH lmg
EIAAB40431 ARSC1,Arylsulfatase C,ASC,Homo sapiens,Human,Steroid sulfatase,Steryl-sulfatase,Steryl-sulfate sulfohydrolase,STS
EIAAB40430 Arylsulfatase C,ASC,Rat,Rattus norvegicus,Steroid sulfatase,Steryl-sulfatase,Steryl-sulfate sulfohydrolase,Sts
EIAAB40429 Arylsulfatase C,ASC,Mouse,Mus musculus,Steroid sulfatase,Steryl-sulfatase,Steryl-sulfate sulfohydrolase,Sts
C270 Human N-Sulphoglucosamine Sulphohydrolase SGSH l0
C154 Human N-Sulphoglucosamine Sulphohydrolase SGSH 50
CSB-EL021200HU Human N-sulphoglucosamine sulphohydrolase(SGSH) ELISA kit 96T
CSB-EL021200HU Human N-sulphoglucosamine sulphohydrolase(SGSH) ELISA kit SpeciesHuman 96T
CA15 Recombinant Human N-Sulphoglucosamine Sulphohydrolase per SGSH (C-6His) 10ug
EIAAB39552 Homo sapiens,HSS,Human,N-sulphoglucosamine sulphohydrolase,SGSH,Sulfoglucosamine sulfamidase,Sulphamidase
Q-1880.0001 Agmatine · sulfate Salt _ Binding _ Synonym Argamine · sulfate, 4_Guanidino_butylamine · sulfate SumFormula C5H14N4 · H2SO4 1.0 g
Q-1880.0005 Agmatine · sulfate Salt _ Binding _ Synonym Argamine · sulfate, 4_Guanidino_butylamine · sulfate SumFormula C5H14N4 · H2SO4 5.0 g
26-191 GALNAC4S-6ST is a sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms 0.05 mg
AHP1670 GOAT ANTI HUMAN ARYLSULFATASE A , Product Type Polyclonal Antibody, Specificity ARYLSULFATASE A, Target Species Human, Host Goat, Format Purified, Isotypes Polyclonal IgG, Applications E, WB, C 0.1 mg
SCH-AHP1670 GOAT ANTI HUMAN ARYLSULFATASE A , Product Type Polyclonal Antibody, Specificity ARYLSULFATASE A, Target Species Human, Host Goat, Format Purified, Isotypes Polyclonal IgG, Applications E, WB, C 0.1 mg
30-071 CHST1 catalyzes the transfer of sulfate to position 6 of galactose (Gal) residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer 0.1 mg
30-488 CHST14 belongs to the sulfotransferase 2 family. CHST14 catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate. It transfers sulfate to the C 0.05 mg
EIAAB40115 Aryl sulfotransferase,Aryl sulfotransferase IV,ASTIV,Minoxidil sulfotransferase,Mx-ST,Phenol sulfotransferase,PST-1,Rat,Rattus norvegicus,ST1A1,St1a1,Sulfokinase,Sulfotransferase 1A1,Sult1a1,Tyrosine-
orb60832 Atazanavir sulfate Atazanavir sulfate(BMS-232632-05) is a sulfate salt form of atazanavir (BMS-232632) that is an highly potent HIV protease inhibitor with an EC50 and EC90 of 2.6~5.3 nM and 9~15 nM i 10 mg
EIAAB09627 Chondroitin sulfate proteoglycan 4,Chondroitin sulfate proteoglycan NG2,CSPG4,Homo sapiens,Human,MCSP,Melanoma chondroitin sulfate proteoglycan,Melanoma-associated chondroitin sulfate proteoglycan
I225000 O-(α-L-Idopyranosyluronic Acid 2-Sulfate-(1-4)-2,5-anhydro-Mannitol-6-sulfate C12H20O17S2 CAS: 69180-27-4 1 mg
I225003 O-(α−L-Idopyranosyluronic Acid 2-Sulfate-(1-4)-2,5-anhydro-D-[3H]- mannitol-6-sulfate C12H19TO17S2 CAS: 10


 

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