| Chapter title |
Methods for Determining Glycosyltransferase Kinetics
|
|---|---|
| Chapter number | 6 |
| Book title |
Protein-Carbohydrate Interactions
|
| Published in |
Methods in molecular biology, April 2017
|
| DOI | 10.1007/978-1-4939-6899-2_6 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-6898-5, 978-1-4939-6899-2
|
| Authors |
Maria Ngo, Michael D. L. Suits |
| Editors |
D. Wade Abbott, Alicia Lammerts van Bueren |
| Abstract |
Glycosyltransferases are a class of biosynthetic enzymes that transfer individual activated monosaccharide units to specific acceptors. Colorimetric assays using the detection of released products such as para-nitrophenol and coupled assays for inorganic phosphate detection allow for convenient and quantifiable kinetic characterization. These techniques may be applied to determine the enzymatic activity of glycosyltransferases by indirectly measuring the transfer of nucleotide-activated donor carbohydrate units to various cognate acceptor molecules. In addition to an overview of these methods, the protocol for quantifying the glycosyltransferase activity used for the characterization of penicillin-binding proteins (PBPs) involving the transfer of lipid II to form elongated murein chains during bacterial cell wall synthesis is described herein. |
Mendeley readers
Geographical breakdown
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|---|---|---|
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Demographic breakdown
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|---|---|---|
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| Student > Bachelor | 2 | 29% |
| Unspecified | 1 | 14% |
| Student > Doctoral Student | 1 | 14% |
| Researcher | 1 | 14% |
| Other | 0 | 0% |
| Readers by discipline | Count | As % |
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| Unspecified | 1 | 14% |
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| Other | 1 | 14% |