Identification of key amino acid residues in Neisseria polysaccharea amylosucrase.
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Sarcabal P, Remaud-Simeon M, Willemot R, Potocki de Montalk G, Svensson B, Monsan P
Identification of key amino acid residues in Neisseria polysaccharea amylosucrase.
FEBS Lett. 2000 May 26;474(1):33-7.
- PubMed ID
- 10828446 [ View in PubMed]
- Abstract
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.