Related Experiment Video
Updated: Feb 7, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
A mechanism for bistability in glycosylation
Andrew G McDonald1, Keith F Tipton1, Gavin P Davey1
1School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.
Abstract:
Glycosyltransferases are a class of enzymes that catalyse the posttranslational modification of proteins to produce a large number of glycoconjugate acceptors from a limited number of nucleotide-sugar donors. The products of one glycosyltransferase can be the substrates of several other enzymes, causing a combinatorial explosion in the number of possible glycan products. The kinetic behaviour of systems where multiple acceptor substrates compete for a single enzyme is presented, and the case in which high concentrations of an acceptor substrate are inhibitory as a result of abortive complex formation, is shown to result in non-Michaelian kinetics that can lead to bistability in an open system. A kinetic mechanism is proposed that is consistent with the available experimental evidence and provides a possible explanation for conflicting observations on the β-1,4-galactosyltransferases. Abrupt switching between steady states in networks of glycosyltransferase-catalysed reactions may account for the observed changes in glycosyl-epitopes in cancer cells.
Related Concept Videos
Protein Glycosylation
Glycosylation occurs in...
Reaction Mechanisms
For instance, the decomposition of ozone appears to follow a mechanism with two steps:
Mechanical Protein Functions
Mechanism of Conjugation
Mechanism of Angiogenesis
An Introduction to Mechanics
According to records, the history of mechanics starts with Aristotle (384–322 BC). He related mechanics to physical theory, aiming for a universal synthesis.
Newton defined mechanics as the branch of physical science that...

