Entry
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
BRITE hierarchy
Sysname
aryl-sulfate sulfohydrolase
Reaction(IUBMB)
an aryl sulfate + H2O = a phenol + sulfate [RN:
R01243 ]
Reaction(KEGG)
Substrate
Product
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
Orthology
Genes
PABY : Ga0080574_TMP478 Ga0080574_TMP494
PCAY : FRD00_07775 FRD00_27270
BACA : FAY30_21980 FAY30_26840
PAEF : R50345_17625 R50345_17630
PAEJ : H70737_17455 H70737_17460
PBK : Back11_15510 Back11_42790
PALO : E6C60_0776 E6C60_0797 E6C60_3608
PSPN : L1F29_16715 L1F29_16720 L1F29_19060 L1F29_22910 L1F29_26470
PKP : SK3146_01136 SK3146_01592 SK3146_01595 SK3146_01876 SK3146_03008 SK3146_05608
BHAN : CGC63_02880 CGC63_03295
VPY : HZI73_07275 HZI73_08065 HZI73_10800 HZI73_14370
CSTC : LK434_01995 LK434_06575
BCV : Bcav_0304 Bcav_0569 Bcav_1300
BRX : BH708_16510 BH708_16895
BRZ : CFK38_00615 CFK38_16445
HALT : IM660_02155 IM660_12510 IM660_13715 IM660_17030 IM660_17360 IM660_18100 IM660_19155
RHAL : LQF10_06845 LQF10_16870
MIK : FOE78_08600 FOE78_09660 FOE78_09710
RUFI : K0V07_04670 K0V07_16095
PUO : RZN69_06435 RZN69_09220 RZN69_14100
MTAR : DF168_00408 DF168_00728(betC_2) DF168_01173
LCRE : Pla8534_36380 Pla8534_56540(atsA_47) Pla8534_62320
PND : Pla175_12770(betC_4) Pla175_23510 Pla175_32370 Pla175_48660(betC_25)
MRI : Mal4_27360 Mal4_29420 Mal4_30210 Mal4_58780(betC_22)
PHM : PSMK_09670 PSMK_11570 PSMK_27950
MCAD : Pan265_03490 Pan265_04460 Pan265_13720
PBU : L21SP3_00903 L21SP3_01497
PBAS : SMSP2_00826 SMSP2_02069
TAER : GT409_04395 GT409_07575 GT409_07990 GT409_10360 GT409_13370 GT409_13400
SASS : MUG09_02450 MUG09_03425
BHC : JFL75_01475 JFL75_14310 JFL75_20605
PFER : IRI77_03680 IRI77_30330
HRR : HZS55_14555 HZS55_14595 HZS55_14625
» show all
Taxonomy
Reference
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
Reference
Authors
WEBB EC, MORROW PF.
Title
The activation of an arysulphatase from ox liver by chloride and other anions.
Journal
Reference
Authors
ROY AB.
Title
The synthesis and hydrolysis of sulfate esters.
Journal
Reference
Authors
Roy AB.
Title
Sulphatases, lysosomes and disease.
Journal
Reference
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
Reference
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
Other DBs
ExplorEnz - The Enzyme Database: 3.1.6.1
ExPASy - ENZYME nomenclature database: 3.1.6.1
BRENDA, the Enzyme Database: 3.1.6.1
LinkDB
All DBs