Identification of key amino acid residues in Neisseria polysaccharea amylosucrase

Patricia Sarcabal, Magali Remaud-Simeon, René-Marc Willemot, Gabrielle Potocki de Montalk, Birte Svensson, Pierre Monsan

Research output: Contribution to journalJournal articleResearchpeer-review


Amylosucrase from Neisseria polysaccharea catalyzes the synthesis of an amylose-like polymer from sucrose. Sequence alignment revealed that it belongs to the glycoside hydrolase family 13. Site-directed mutagenesis enabled the identification of functionally important amino acid residues located at the active center. Asp-294 is proposed to act as the catalytic nucleophile and Glu-336 as general acid base catalyst in amylosucrase. The conserved Asp-401, His-195 and His-400 residues are critical for the enzymatic activity. These results provide strong support for the predicted close structural and functional relationship between the sucrose-glucosyltransferases and enzymes of the alpha-amylase family.
Original languageEnglish
JournalF E B S Letters
Pages (from-to)33-37
Publication statusPublished - 2000
Externally publishedYes

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