Abstract
The development of a general 1-Zn(II) nucleoside diphosphate (NDP) sensor assay for rapid evaluation of glycosyltransferase (GT) activity is described. The 1-Zn(II) NDP sensor assay offers submicromolar sensitivity, compatibility with both purified enzymes and crude cell extracts, and exquisite selectivity for NDPs over the corresponding NDP-sugars. Thus, the 1-Zn(II) NDP sensor assay is anticipated to offer broad applicability in the context of GT engineering and characterization.
| Original language | English |
|---|---|
| Pages (from-to) | 85-88 |
| Number of pages | 4 |
| Journal | Analytical Biochemistry |
| Volume | 418 |
| Issue number | 1 |
| DOIs | |
| State | Published - Nov 1 2011 |
Bibliographical note
Funding Information:This work was supported by funding from the NIH ( AI52218 ) and the Laura and Edward Kremers Chair in Natural Products Chemistry (J.S.T.).
Funding
This work was supported by funding from the NIH ( AI52218 ) and the Laura and Edward Kremers Chair in Natural Products Chemistry (J.S.T.).
| Funders | Funder number |
|---|---|
| National Institutes of Health (NIH) | |
| National Institute of Allergy and Infectious Diseases | R01AI052218 |
Keywords
- Carbohydrate
- Engineering
- Enzyme
- Evolution
- Glycosyltransferase
- Sugar nucleotide
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology