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Demonstration of a novel sulfotransferase in fetal bovine serum, which transfers sulfate to the C6 position of the GalNAc residue in the sequence iduronic acidα1‐3GalNAcβ1‐4iduronic acid in dermatan sulfate
Author(s) -
Nadanaka Satomi,
Fujita Masaki,
Sugahara Kazuyuki
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00597-9
Subject(s) - iduronic acid , sulfotransferase , dermatan sulfate , chemistry , sulfation , biochemistry , enzyme , chondroitin , residue (chemistry) , glucuronic acid , stereochemistry , chondroitin sulfate , heparan sulfate , glycosaminoglycan , polysaccharide
A novel sulfotransferase activity was discovered in fetal bovine serum using pig skin dermatan sulfate as an acceptor and [ 35 S]3′‐phosphoadenosine 5′‐phosphosulfate as a sulfate donor. The enzyme was separated from chondroitin:GalNAc 6‐ O ‐sulfotransferase by chromatographic techniques. Enzymatic analysis of the reaction products demonstrated that the enzyme transferred sulfate to the C6 position of the GalNAc residue in the sequence ‐iduronic acidα1‐3GalNAcβ1‐4iduronic acid‐. Thus, the enzyme has been identified as a hitherto unreported dermatan sulfate:GalNAc 6‐ O ‐sulfotransferase. The finding is in sharp contrast to the current concept that in dermatan sulfate biosynthesis GalNAc 4‐ O ‐sulfation is a prerequisite for iduronic acid formation by C5 epimerase.