Structural investigation of the thermostability and product specificity of amylosucrase from the bacterium Deinococcus geothermalis.

ABSTRACT: Amylosucrases are sucrose-utilizing α-transglucosidases that naturally catalyze the synthesis of α-glucans, linked exclusively through α1,4-linkages. Side products and in particular sucrose isomers such as turanose and trehalulose are also produced by these enzymes. Here, we report the first structural and biophysical characterization of the most thermostable amylosucrase identified so far, the amylosucrase from Deinoccocus geothermalis (DgAS). The three-dimensional structure revealed a homodimeric quaternary organization, never reported before for other amylosucrases. A sequence signature of dimerization was identified from the analysis of the dimer interface and sequence alignments. By rigidifying the DgAS structure, the quaternary organization is likely to participate in the enhanced th

SUBMITTER: Guerin F 

PROVIDER: S-EPMC3307298 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature