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3.1.6.1: arylsulfatase (type I)

This is an abbreviated version!
For detailed information about arylsulfatase (type I), go to the full flat file.

Word Map on EC 3.1.6.1

Reaction

an aryl sulfate
+
H2O
=
a phenol
+
sulfate

Synonyms

4-methylumbelliferyl sulfatase, ARS, ARS-A, ARS-B, ARSA, ARSB, ARSE, ARSK, ary 423, Aryl-sulfate sulphohydrolase, arylsufatase B, arylsulfatase, arylsulfatase A, arylsulfatase B, arylsulfatase E, arylsulfatase Es-2, arylsulfatase G, arylsulfatase gene, arylsulfatase III, arylsulfatase J, arylsulfatase K, arylsulfatase type VI, arylsulfate sulfohydrolase II, arylsulfohydrolase, arylsulphatase, arylsulphatase A, AS-A, ASG, AstA, AtsA, estrogen sulfatase, KIAA1001, nitrocatechol sulfatase, p-nitrophenyl sulfatase, P70, PAS, phenolsulfatase, phenylsulfatase, sulfatase, sulfatase, aryl-

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.6 Sulfuric-ester hydrolases
                3.1.6.1 arylsulfatase (type I)

Posttranslational Modification

Posttranslational Modification on EC 3.1.6.1 - arylsulfatase (type I)

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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
no modification
-
not a glycoprotein
proteolytic modification
side-chain modification
-
formylglycine is generated by posttranslational modification of a conserved cysteine residue. Cysteine is also converted to formylglycine when the gene is expressed in Escherichia coli. Substituting the relevant cysteine by a serine codon in the gene of Pseudomonas aeruginosa leads to expression of inactive sulfatase protein, lacking the formylglycine. The machinery catalyzing the modification of the Pseudomonas sulfatase in E. coli therefore accepts cysteine but not serine as a modification substrate
additional information