The effect of N-linked glycosylation on the substrate preferences of UDP glucuronosyltransferases

Biochemical and Biophysical Research Communications
P I Mackenzie

Abstract

The presence of potential N-linked glycosylation sites (Asn-X-Ser/Thr) in two forms of UDP glucuronosyltransferase, designated UDPGTr-2 and UDPGTr-4, has been deduced from cDNA sequence data. These forms were glycosylated when synthesized from expression vectors transfected into COS cells and were converted to faster migrating species on SDS polyacrylamide gels when treated with endoglycosidase H. The role of glycosylation was investigated by determining the substrate specificities and stabilities of the glycosylated enzymes and their unglycosylated variants which were synthesized in the presence of tunicamycin. Analysis of the activities towards 13 different aglycones showed that the glycosyl moiety was not essential for catalytic activity and had no effect on the substrate preference of each form. The stabilities of the proteins were not adversely affected by the absence of this posttranslational modification. A possible effect of N-linked oligosaccharides on the catalytic properties of these two forms of UDP glucuronosyltransferase is discussed.

References

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Citations

Dec 1, 1992·The Journal of Steroid Biochemistry and Molecular Biology·P I MackenzieS Stranks
Aug 29, 2003·The Journal of Steroid Biochemistry and Molecular Biology·Olivier Barbier, Alain Bélanger
Dec 24, 1997·Clinical and Experimental Pharmacology & Physiology·R Meech, P I Mackenzie
Jan 14, 2012·Drug Metabolism and Pharmacokinetics·Kenjiro NagaokaShizuo Narimatsu
Dec 3, 2009·Biochemical Pharmacology·Miki NakajimaTsuyoshi Yokoi
Oct 27, 2016·Drug Metabolism and Disposition : the Biological Fate of Chemicals·Camille Girard-BockChantal Guillemette
May 5, 2020·Glycobiology·Krzysztof MikolajczykMarcin Czerwinski

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