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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Hlavní autoři: Saburi, Wataru, Kobayashi, Momoko, Mori, Haruhide, Okuyama, Masayuki, Kimura, Atsuo
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2013
Témata:
Enzymology
On-line přístup: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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