Chondroitin 6-sulfotransferase, EC 2.8.2.17, uses PAPS to modify the 6-position of N-acetylgalactosamine residues in chondroitin. Its products include chondroitin 6-sulfate and adenosine 3',5'-bisphosphate. The 6-position specifies the acceptor site and distinguishes the activity from chondroitin 4-sulfotransferase.[ref]
Chondroitin 6-sulfotransferase in IUBMB Enzyme Nomenclature. Reaction, Systematic name and Comments
A constructed pair of polymer samples illustrates why position matters independently of amount. Suppose two otherwise matched populations each contain one hundred eligible sugar positions and forty newly attached sulfate groups. If the groups occupy position 4 in the first population and position 6 in the second, the group counts and elemental additions agree while their attachment locations differ. Measuring the count alone cannot choose between the two structures.
The 1982 study of chick embryo cartilage provides a concrete biochemical comparison. The separated 6-sulfotransferase and 4-sulfotransferase activities differed in solubility behavior and in responses to assay components. Removing endogenous acceptors from the preparations helped make the supplied acceptor part of an interpretable activity measurement.[ref]
Separation and characterization of chondroitin 6-sulfotransferase and chondroitin 4-sulfotransferase from chick embryo cartilage by O. Habuchi and N. Miyashita. Abstract, separation, acceptor removal and differing properties
An activity measurement must consequently state the acceptor and assay conditions, rather than infer activity from the amount of protein present. The shared PAPS donor and related polymer substrates create a need for positional product characterization. Chondroitin synthase, which extends the sugar backbone, answers another chemical question: the sulfotransferase modification does not by itself add another sugar residue.
Articles by others on the same topic
There are currently no matching articles.