X4 Modules Represent a New Family of Carbohydrate-binding Modules That Display Novel Properties

Autor: Bernard Henrissat, David N. Bolam, Harry J. Gilbert, H. Xie, Greta Galbraith, Gavin Pell, Deborah Hogg

Publikováno v: Journal of Biological Chemistry. 279:22953-22963

The hydrolysis of the plant cell wall by microbial glycoside hydrolases and esterases is the primary mechanism by which stored organic carbon is utilized in the biosphere, and thus these enzymes are of considerable biological and industrial importanc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cdc31d8d5decaf52f93985193a8b8fb
https://doi.org/10.1074/jbc.m313317200

Multifunctional Xylooligosaccharide/Cephalosporin C Deacetylase Revealed by the Hexameric Structure of the Bacillus subtilis Enzyme at 1.9Å Resolution

Autor: Johan P. Turkenburg, Koen H.G. Verschueren, Gideon J. Davies, Gavin Pell, Shirley M. Roberts, Harry J. Gilbert, James A. Brannigan, David J. Scott, Wendy A. Offen, Florence Vincent, Simon J. Charnock

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, 2003, 330 (3), pp.593-606. ⟨10.1016/s0022-2836(03)00632-6⟩
Journal of Molecular Biology, Elsevier, 2003, 330 (3), pp.593-606. ⟨10.1016/s0022-2836(03)00632-6⟩

Esterases and deacetylases active on carbohydrate ligands have been classified into 14 families based upon amino acid sequence similarities. Enzymes from carbohydrate esterase family seven (CE-7) are unusual in that they display activity towards both

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4e1ea814eb0cee34658d986ae16f90e
https://doi.org/10.1016/s0022-2836(03)00632-6

Mycobacterium tuberculosis strains possess functional cellulases

Autor: James M. Macdonald, Annabelle Varrot, Sabine Leydier, Gideon J. Davies, Bernard Henrissat, Harry J. Gilbert, Robert V. Stick, Gavin Pell

Publikováno v: The Journal of biological chemistry. 280(21)

The genomes of various Mycobacterium tuberculosis strains encode proteins that do not appear to play a role in the growth or survival of the bacterium in its mammalian host, including some implicated in plant cell wall breakdown. Here we show that M.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e3e4e1d018e44f18c4b3e8ebe6fbdf1
https://pubmed.ncbi.nlm.nih.gov/15824123

Structure of a mannan-specific family 35 carbohydrate-binding module: evidence for significant conformational changes upon ligand binding

Autor: Gavin Pell, David N. Bolam, Harry J. Gilbert, Richard B. Tunnicliffe, Michael P. Williamson

Publikováno v: Journal of molecular biology. 347(2)

Enzymes that digest plant cell wall polysaccharides generally contain non-catalytic, carbohydrate-binding modules (CBMs) that function by attaching the enzyme to the substrate, potentiating catalytic activity. Here, we present the first structure of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d924646f24e0f11771370244ca85e4a7
https://pubmed.ncbi.nlm.nih.gov/15740741

Insights into the Molecular Determinants of Substrate Specificity in Glycoside Hydrolase Family 5 Revealed by the Crystal Structure and Kinetics of Cellvibrio mixtus Mannosidase 5A

Autor: Louise E. Tailford, Florence Vincent, Luís M. A. Ferreira, Maria S.J. Centeno, José A. M. Prates, Fernando M. V. Dias, Gavin Pell, Gideon J. Davies, Harry J. Gilbert, Carlos M. G. A. Fontes

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279 (24), pp.25517-25526. ⟨10.1074/jbc.M401647200⟩
Journal of Biological Chemistry, 2004, 279 (24), pp.25517-25526. ⟨10.1074/jbc.m401647200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279 (24), pp.25517-25526. ⟨10.1074/jbc.m401647200⟩

The enzymatic hydrolysis of the glycosidic bond is central to numerous biological processes. Glycoside hydrolases, which catalyze these reactions, are grouped into families based on primary sequence similarities. One of the largest glycoside hydrolas

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa26012056ec46bdb90e64c6bd8f59f1
https://hal.archives-ouvertes.fr/hal-03281304