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
ec01100  Metabolic pathways
Orthology
K01130  arylsulfatase
Genes
KLWDA718_20290
ETEETEE_3380
EDWQY76_12995
EDLAAZ33_07220
GAIIMCC3135_09555
HHUAR456_01895
PCAFDSC91_007680
BBROBAU06_00040 BAU06_05825
BOHAKI39_13145
ACHRC2U31_06605
AKATKWG_21235
PCAYFRD00_07775 FRD00_27270
MESMEJ066_13465
RJGCCGE525_31715 CCGE525_31725
RHRCKA34_30115
NGLRG1141_PA09260 RG1141_PA12920
NGGRG540_PA08240 RG540_PA13910
NENNCHU2750_53620
BGZXH91_30815
BARHWN72_43370
MOCBB934_10175
PHLKKY_3091 KKY_3092
MEYTM49_15780
MAADAZF01_09150
MMEDMame_04823
MALGMALG_00822
PABYGa0080574_TMP478 Ga0080574_TMP494
BOOE2K80_04590 E2K80_11615
PPAFI8N54_04630 I8N54_18025
CMAGCBW24_06020
FAPGR316_13240
BACAFAY30_21980 FAY30_26840
VIRX953_15095
VHLBME96_14445
VILCFK37_08495
MEKUHUW50_24170
BLENNCTC4824_01157 NCTC4824_01489
SSDSPSINT_0710
SDTSPSE_1822
SDPNCTC12225_02043
SFQC7J90_06785
SLLOISP08_12545
PJDPjdr2_3275
GYMGYMC10_3591
PODPODO_17545
PAEFR50345_17625 R50345_17630
PAEJH70737_17455 H70737_17460
PIBBBD41_05085
PVOPVOR_18444
PLWD5F53_12285
PALBEJC50_09000
PBKBack11_15510 Back11_42790
PRZGZH47_23540 GZH47_30135
PLYCGXP70_14480
PALOE6C60_0776 E6C60_0797 E6C60_3608
SPWSPCG_1785
SJJSPJ_1708
SNVSPNINV200_16270
SNESPN23F18200
SPVSPH_1924
SNMSP70585_1861
SNIINV104_15470
SPNGHMPREF1038_01772
SNPSPAP_1798
SNXSPNOXC15830
SNUSPNA45_00441
SPNUSPN034183_15850
SPNMSPN994038_15740
SPNOSPN994039_15750
SACOSAME_00562
LCSLCBD_0376
LCELC2W_0372
LCWBN194_03810
LCBLCABL_03730
LCTBI355_0118
EFLEF62_2204
EFUHMPREF0351_12962
ESGEsVE80_00870
ECECNCTC12421_00037
ADCFOC79_05975
GADK8O88_02400
CPECPE0231
CPFCPF_0221
HHJNQ487_28975
FSAC5Q98_04645
RUKA4V00_18535
CAPREQM14_02105
PFAAMM59RIKEN_16380
BHANCGC63_02880 CGC63_03295
CSHClosa_2327
SINTK5I26_04290
MFORNQ534_12375
VGUHYG85_17990
VPYHZI73_07275 HZI73_07905 HZI73_08045 HZI73_08065 HZI73_10800 HZI73_14370
AARGAargi30884_25930
ABSIA9CBEGH2_23250
CIUG4D55_14905
LCGL3BBH23_22600
ERBA4V01_18005
SALFSMD44_02010
SASTCD934_00820
SAOVG3H79_29075
MHOSCXR34_01585
MCHNHCR76_11955
AMAUDSM26151_12600
ARRARUE_c16440
ARMART_4143
AREAL755_08370
ARWMB46_08130
AAUAAur_1732
PNVJMY29_08245
BCVBcav_0304 Bcav_0569 Bcav_1300
BFABfae_06030 Bfae_28180
BRXBH708_10430 BH708_16095 BH708_16510 BH708_16895
BRVCFK39_11060
BGGCFK41_13840
BRZCFK38_00615 CFK38_16445
BSAUDWV08_16075
BKIM4486_12950 M4486_17220
BRHANLU66_17500
BHHBra3105_13905
LMOIVV02_08325
HALTIM660_01935 IM660_02155 IM660_12510 IM660_13715 IM660_17030 IM660_17360 IM660_18100 IM660_19155
RHALLQF10_06845 LQF10_16870
RSUALQF12_10315
MIKFOE78_08600 FOE78_09660 FOE78_09710
MICGGJV80_01260
TESBW730_09190
TDFH9L22_01550
NOWGBF35_41150
PSEEFRP1_09870
PSEQAD006_17430
PECQAD017_25265
PHHAFB00_15765 AFB00_17025 AFB00_28850
VERHUT12_13375
AREPID810_07800
CSTCLK434_01995 LK434_06575
RUFIK0V07_04670 K0V07_16095
RMLFF011L_10200
AHELQ31a_10040 Q31a_30530
LCREPla8534_23680 Pla8534_36380 Pla8534_56540(atsA_47) Pla8534_62320
AAGGETAA8_66950
RLCK227x_25550
AMUCPan181_48500
PNDPla175_12770(betC_4) Pla175_23510 Pla175_32370 Pla175_48660(betC_25)
PBSPlabr_1085
FMRFuma_01030
GMRGmarT_19840
GIMF1728_04980 F1728_19830
GPNPan110_19390 Pan110_44510
MRIMal4_27360 Mal4_29420 Mal4_30210 Mal4_46690 Mal4_58780(betC_22)
SDYNMal52_08690 Mal52_40630
PLONPla110_05160
TSPHKIH39_01535
PHMPSMK_09670 PSMK_11570 PSMK_27950
MCADPan265_03490 Pan265_04460 Pan265_13720
PBUL21SP3_00903 L21SP3_01497
PBPSTSP1_01495
PBASSMSP2_00826 SMSP2_01427 SMSP2_02069
ALUSSTSP2_02144
VBLL21SP4_02331
TAERGT409_04395 GT409_07575 GT409_07990 GT409_10360 GT409_13370 GT409_13400
TBETrebr_2355
SBUSpiBuddy_0360
SASSMUG09_02450 MUG09_03425
BHCJFL75_01475 JFL75_14310 JFL75_20605
BHYBHWA1_00429
BHDBHYOB78_01035
BRMBmur_0151
BIPBint_1411
BHPBHAMNSH16_00780
EDAGWR55_15335
EDGH7846_14450
SUSAcid_7475
PFERIRI77_03680 IRI77_30330
FVAFV113G1_27040
FULC4N20_10170
FMOC4N19_13235
STRSterm_2100
BTHBT_1918
BTHOBtheta7330_01094
BFRBF0070
BFSBF9343_0080
BFGBF638R_0067
BFBVU15_21615
BCACCGC64_09985
BNOK8P02_17955
BVUBVU_3788
BDOEL88_11875
BDHGV66_19545
PCOPI6J50_11325
DYSG7050_15260
PDIBDI_2610
PARCCI960_19260
PMERINE87_01848
PGOLK6V26_01490
PJOLK449_13010
RBCBN938_1433
MCOSGM418_29000
ARKD6B99_12925
AGDFRZ59_08675
FKAKM029_23770
AALGAREALGSMS7_03288
GAAHX109_09160
HRRHZS55_14555 HZS55_14595 HZS55_14625 HZS55_14630
HPELHZS54_10725
HDOMUK72_15915
HALGHUG10_15510
HLRHALLA_01810
SAWLNGM29_11665
 » 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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