KEGG   ENZYME: 3.1.6.1
Entry
EC 3.1.6.1                  Enzyme                                 

Name
arylsulfatase (type I);
sulfatase;
nitrocatechol sulfatase;
phenolsulfatase;
phenylsulfatase;
p-nitrophenyl sulfatase;
arylsulfohydrolase;
4-methylumbelliferyl sulfatase;
estrogen sulfatase;
type I sulfatase;
arylsulfatase
Class
Hydrolases;
Acting on ester bonds;
Sulfuric-ester hydrolases
Sysname
aryl-sulfate sulfohydrolase
Reaction(IUBMB)
an aryl sulfate + H2O = a phenol + sulfate [RN:R01243]
Reaction(KEGG)
R01243 > R03980;
(other) R04856 R06280(G)
Substrate
aryl sulfate [CPD:C00850];
H2O [CPD:C00001]
Product
phenol [CPD:C15584];
sulfate [CPD:C00059]
Comment
Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-beta-lactamase fold and binds two zinc ions as cofactors. Arylsulfatases are type I enzymes, found in both prokaryotes and eukaryotes, with rather similar specificities. The key catalytic residue 3-oxo-L-alanine initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate. This residue is generated by posttranslational modification of a conserved cysteine or serine residue by EC 1.8.3.7, formylglycine-generating enzyme, EC 1.1.98.7, serine-type anaerobic sulfatase-maturating enzyme, or EC 1.8.98.7, cysteine-type anaerobic sulfatase-maturating enzyme.
History
EC 3.1.6.1 created 1961, modified 2011, modified 2021
Pathway
ec00140  Steroid hormone biosynthesis
ec00600  Sphingolipid metabolism
Orthology
K01130  arylsulfatase
Genes
KLW: DA718_20290
ETE: ETEE_3380
EDW: QY76_12995
EDL: AAZ33_07220
GAI: IMCC3135_09555
HHU: AR456_01895
PCAF: DSC91_007680
BBRO: BAU06_00040 BAU06_05825
BOH: AKI39_13145
ACHR: C2U31_06605
BARH: WN72_43370
MMED: Mame_04823
MALG: MALG_00822
SDT: SPSE_1822
SPW: SPCG_1785
SJJ: SPJ_1708
SPV: SPH_1924
SNP: SPAP_1798
LCS: LCBD_0376
LCE: LC2W_0372
EFL: EF62_2204
CPE: CPE0231
CPF: CPF_0221
ARM: ART_4143
AAU: AAur_1732
LMOI: VV02_08325
PSEE: FRP1_09870
BRM: Bmur_0151
BIP: Bint_1411
SUS: Acid_7475
BTH: BT_1918
BFR: BF0070
BVU: BVU_3788
PDI: BDI_2610
 » show all
Reference
1  [PMID:13363831]
  Authors
DODGSON KS, SPENCER B, WILLIAMS K.
  Title
Studies on sulphatases.  13.  The hydrolysis of substituted phenyl sulphates by the arylsulphatase of Alcaligenes metalcaligenes.
  Journal
Biochem J 64:216-21 (1956)
DOI:10.1042/bj0640216
Reference
2  [PMID:13843260]
  Authors
WEBB EC, MORROW PF.
  Title
The activation of an arysulphatase from ox liver by chloride and other anions.
  Journal
Biochem J 73:7-15 (1959)
DOI:10.1042/bj0730007
Reference
3  [PMID:13744184]
  Authors
ROY AB.
  Title
The synthesis and hydrolysis of sulfate esters.
  Journal
Adv Enzymol Relat Subj Biochem 22:205-35 (1960)
DOI:10.1002/9780470122679.ch5
Reference
4  [PMID:13772]
  Authors
Roy AB.
  Title
Sulphatases, lysosomes and disease.
  Journal
Aust J Exp Biol Med Sci 54:111-35 (1976)
DOI:10.1038/icb.1976.13
Reference
5  [PMID:7628016]
  Authors
Schmidt B, Selmer T, Ingendoh A, von Figura K.
  Title
A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency.
  Journal
Cell 82:271-8 (1995)
DOI:10.1016/0092-8674(95)90314-3
Reference
6  [PMID:9748219]
  Authors
Dierks T, Miech C, Hummerjohann J, Schmidt B, Kertesz MA, von Figura K
  Title
Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine.
  Journal
J Biol Chem 273:25560-4 (1998)
DOI:10.1074/jbc.273.40.25560
Other DBs
ExplorEnz - The Enzyme Database: 3.1.6.1
IUBMB Enzyme Nomenclature: 3.1.6.1
ExPASy - ENZYME nomenclature database: 3.1.6.1
BRENDA, the Enzyme Database: 3.1.6.1
CAS: 9016-17-5
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