The cofactor Mg2+—a key switch for effective continuous enzymatic production of GDP-mannose using recombinant GDP-mannose pyrophosphorylase
- 1 December 1997
- journal article
- Published by Elsevier in Carbohydrate Research
- Vol. 305 (3-4) , 475-481
- https://doi.org/10.1016/s0008-6215(97)10095-7
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Chemical transformations employing glycosyltransferasesPublished by Springer Nature ,1997
- Dolichol is not a necessary moiety for lipid-linked oligosaccharide substrates of the mannosyltransferases involved in in vitro N-linked-oligosaccharide assemblyBiochemical Journal, 1995
- Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: a surveyGlycobiology, 1995
- Enzymes in Organic Synthesis: Application to the Problems of Carbohydrate Recognition (Part 2)Angewandte Chemie International Edition in English, 1995
- Large scale production of recombinant .alpha.-1,2-mannosyltransferase from E. coli for the study of acceptor specificity and use of the recombinant whole cells in synthesisThe Journal of Organic Chemistry, 1994
- Enzymes involved in mammalian oligosaccharide biosynthesisCurrent Opinion in Structural Biology, 1994
- Recombinant Whole Cells as Catalysts for the Enzymatic Synthesis of Oligosaccharides and GlycopeptidesAngewandte Chemie International Edition in English, 1994
- A novel mono-branched lipid phosphate acts as a substrate for dolichyl phosphate mannose synthetaseBiochemical Journal, 1993
- Enzyme-catalyzed oligosaccharide synthesisAnalytical Biochemistry, 1992
- Two Decades of Research on Biosynthesis of SaccharidesScience, 1971