Eukaryotic glycosyltransferases: cysteines and disulfides.
Significant progress has been made in discovering and cloning a host of eukaryotic glycosyltransferases, demonstrating the intricacy and complexity of protein and lipid glycosylation. The availability of their predicted amino acid sequences extended our insights into the structure/function aspects of this family of proteins. However, our knowledge of their three-dimensional structures and how structure gives rise to substrate binding and specificity is still limited. Glycosyltransferase X-ray crystal structures have begun to provide significant information on a limited number of enzymes. To date, only three eukaryotic glycosyltransferase crystal structures have been solved, and all of them are for enzymes that utilize a UDP-sugar. One of the important structural elements of a protein is its disulfide bonds. These covalent interactions place conformational constraints on the overall protein structure,providing some important structural information. In this letter, we outline our current understanding of the free Cys residues and disulfide bonds in eukaryotic glycosyltransferases and discuss some of the important outcomes of these findings.
Thomas
Scott
S
Yen
Ten-Yang
TY
Macher
Bruce A
BA
D000818:Animals; D003545:Cysteine / Q000737:chemistry* / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry* / Q000378:metabolism; D005057:Eukaryotic Cells / Q000201:enzymology*; D016695:Glycosyltransferases / Q000737:chemistry* / Q000378:metabolism; D006801:Humans
D004220:Disulfides; D016695:Glycosyltransferases; D003545:Cysteine