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How Does Nature Cleave Sulfuric Acid Esters? A Novel Posttranslational Modification of Sulfatases
Author(s) -
UhlhornDierks Gunther,
Kolter Thomas,
Sandhoff Konrad
Publication year - 1998
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19981002)37:18<2453::aid-anie2453>3.0.co;2-n
Subject(s) - sulfatase , residue (chemistry) , cleave , cysteine , chemistry , enzyme , biochemistry , posttranslational modification , arylsulfatase a , acetylation , stereochemistry , gene
A rare inherited disease , multiple sulfatase deficiency, is attributed to a defect in a posttranslational protein modification which is essential for the catalytic activity of all known sulfatases. Structure analysis of arylsulfatase A, the enzyme that cleaves sulfatide 1 , shows that the modification of a cysteine residue into a formylglycine residue is essential for catalytic activity.