Plant Mol Biol (2016) 92:401–410 DOI 10.1007/s1103-016-0515-21 GH32 family activity: a topological approach through protein contact networks 2 1 3 1 Sara Cimini · Luisa Di Paola · oAlessandr Giuliani · Alessandra Ridolfi · Laura De Gara Received: 2 February 2016 / Accepted: 14 July 2016 / Published online: 8 August 2016 © Springer Science +Business Media Dordrecht 2016 Abstract and in identifying the structural counterpart of the properties Key message The application of Protein Contact Net - of GH32 enzymes, which remain uncertain, like their alloste - works methodology allowed to highlight a novel response ric character. The main outcome of the study was the discov - of border egion r between the two domains to substrate ery of the activation upon binding of the border (cleft) region binding. between the two domains. This reveals the allosteric nature Glycoside hydrolases (GH) are enzymes that of the enzymatic activity for all the analyzed forms in the mainly hydrolyze the glycosidic bond between two carbo - GH32 family, a character yet to be highlighted in biochemi - hydrates or a carbohydrate and a non-carbohydrate moi - cal studies. Furthermore, we have been able to recognize a . These enzymes are involved in
Plant Molecular Biology – Springer Journals
Published: Aug 8, 2016
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