How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity.

Cuskin, Fiona; Flint, James E; Gloster, Tracey M; Morland, Carl; Baslé, Arnaud; Henrissat, Bernard; Coutinho, Pedro M; Strazzulli, Andrea; Solovyova, Alexandra S; Davies, Gideon J; Gilbert, Harry J

Cuskin, Fiona; Flint, James E; Gloster, Tracey M; Morland, Carl; Baslé, Arnaud; Henrissat, Bernard; Coutinho, Pedro M; Strazzulli, Andrea; Solovyova, Alexandra S; Davies, Gideon J; Gilbert, Harry J.

Affiliation

Cuskin F; Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom.

Proc Natl Acad Sci U S A ; 109(51): 20889-94, 2012 Dec 18.

Article in En | MEDLINE | ID: mdl-23213210

Subject(s)

Bacillus subtilis/metabolism; Carbohydrates/chemistry; Enzymes/chemistry; Bacteroides/metabolism; Biofuels; Calorimetry/methods; Catalysis; Crystallography, X-Ray/methods; Fructans/chemistry; Glycoside Hydrolases/chemistry; Hydrophobic and Hydrophilic Interactions; Kinetics; Lectins/chemistry; Ligands; Models, Chemical; Oligosaccharides/chemistry; Polysaccharides/chemistry; Protein Binding; Protein Structure, Tertiary

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Full text: 1 Database: MEDLINE Main subject: Bacillus subtilis / Carbohydrates / Enzymes Language: En Journal: Proc Natl Acad Sci U S A Year: 2012 Type: Article Affiliation country: United kingdom

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