Structural determinants of product specificity of sucrose isomerases.

Research paper by Stéphanie S Ravaud, Xavier X Robert, Hildegard H Watzlawick, Richard R Haser, Ralf R Mattes, Nushin N Aghajari

Indexed on: 12 May '09Published on: 12 May '09Published in: FEBS Letters

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Abstract

The healthy sweetener isomaltulose is industrially produced from the conversion of sucrose by the sucrose isomerase SmuA from Protaminobacter rubrum. Crystal structures of SmuA in native and deoxynojirimycin complexed forms completed with modeling studies unravel the characteristics of the isomaltulose synthases catalytic pocket and their substrate binding mode. Comparison with the trehalulose synthase MutB highlights the role of Arg(298) and Arg(306) active site residues and surface charges in controlling product specificity of sucrose isomerases (isomaltulose versus trehalulose). The results provide a rationale for the specific design of optimized enzymes.

Structural determinants of product specificity of sucrose isomerases.

Abstract

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The structural basis of Erwinia rhapontici isomaltulose synthase.

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Structural determinants of product specificity of sucrose isomerases.

Abstract

More like this:

The structural basis of Erwinia rhapontici isomaltulose synthase.

Transgenic expression of trehalulose synthase results in high concentrations of the sucrose isomer trehalulose in mature stems of field-grown sugarcane.

Gene cloning, protein characterization, and alteration of product selectivity for the trehalulose hydrolase and trehalulose synthase from "Pseudomonas mesoacidophila" MX-45.

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