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.
| Predicate | Object |
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| rdf:type | |
| rdfs:comment |
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.
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| skos:exactMatch | |
| uniprot:name |
FEBS Lett.
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| uniprot:author |
Monsan P.,
Potocki de Montalk G.,
Remaud-Simeon M.,
Sarcabal P.,
Svensson B.,
Willemot R.-M.
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| uniprot:date |
2000
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| uniprot:pages |
33-37
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| uniprot:title |
Identification of key amino acid residues in Neisseria polysaccharea amylosucrase.
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| uniprot:volume |
474
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| dc-term:identifier |
doi:10.1016/S0014-5793(00)01567-2
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