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Replacement of the Catalytic Nucleophile Aspartyl Residue of Dextran Glucosidase by Cysteine Sulfinate Enhances Transglycosylation Activity
Dextran glucosidase from Streptococcus mutans (SmDG) catalyzes the hydrolysis of an α-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran. This enzyme has an Asp-194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys-129 and Cys-532. Cys-free Sm...
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| Main Authors: | , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Society for Biochemistry and Molecular Biology
2013
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3814762/ https://ncbi.nlm.nih.gov/pubmed/24052257 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M113.491449 |
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