Probing Substrate Promiscuity of Amylosucrase from Neisseria polysaccharea - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue ChemCatChem Année : 2013

Probing Substrate Promiscuity of Amylosucrase from Neisseria polysaccharea

Résumé

The amylosucrase from Neisseria polysaccharea (NpAS) naturally catalyzes the synthesis of a variety of products from sucrose and shows signs of plasticity of its active site. p-nitrophenyl-alpha D-glucopyranoside was used by the wild-type enzyme, and this underlines the high specificity of the -1 subsite of NpAS for glucosyl donor substrates. D- and L-monosaccharides as well as polyols. With the exception of one compound, all were successfully glucosylated, and this showcases the tremendous plasticity of the +1 subsite of NpAS, which is responsible for acceptor recognition. The products obtained from the transglucosylation reactions of three selected acceptors were characterized, and they revealed original structures and enzyme enantiopreference, which were more particularly analyzed by in silico docking analyses.

Dates et versions

hal-01268441 , version 1 (04-02-2016)

Identifiants

Citer

David Daudé, Sandrine Morel, David Guieysse, Magali Remaud Simeon, Isabelle André. Probing Substrate Promiscuity of Amylosucrase from Neisseria polysaccharea. ChemCatChem, 2013, 5 (8), pp.2288 - 2295. ⟨10.1002/cctc.201300012⟩. ⟨hal-01268441⟩
70 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More