Skip to search formSkip to main contentSkip to account menu
Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
TLDR
The present review summarizes the impact structural biology has had on the understanding of the mechanisms by which CBMs bind to their target ligands.
View on PubMed
Glycosyltransferases: structures, functions, and mechanisms.
TLDR
The expected two-step double-displacement mechanism is rendered less likely by the lack of conserved architecture in the region where a catalytic nucleophile would be expected, and a mechanism involving a short-lived oxocarbenium ion intermediate now seems the most likely, with the leaving phosphate serving as the base.
View on PubMed
Structures and mechanisms of glycosyl hydrolases.
View on PubMed
Structural and sequence-based classification of glycoside hydrolases.
View on PubMed
An evolving hierarchical family classification for glycosyltransferases.
View on PubMed
Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components
TLDR
It is demonstrated that copper is needed for GH61 maximal activity and that the formation of cellodextrin and oxidized cellodesxtrin products by GH61 is enhanced in the presence of small molecule redox-active cofactors such as ascorbate and gallate.
View on Publisher
Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification
TLDR
The three‐dimensional structure of VvGT1 has been determined, both in its ‘Michaelis’ complex with a UDP‐glucose‐derived donor and the acceptor kaempferol and in complex with UDP and quercetin, providing the foundation for understanding the mechanism of these enzymes in small molecule homeostasis.
View on Wiley
A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo.
TLDR
Thiamet-G will find wide use in probing the functional role of O-GlcNAc in vertebrate brain, and it may also offer a route to blocking pathological hyperphosphorylation of tau in AD.
View on PubMed
Crystal structure of an N-terminal fragment of the DNA gyrase B protein
The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, com-plexed with a nonhn/drolysable ATP analogue, has been solved at 2.5 Å resolution. It consists of two…
View on Nature
Crystal structure of levansucrase from the Gram-negative bacterium Gluconacetobacter diazotrophicus.
TLDR
A comparison of both structures, the mutagenesis data and the analysis of GH68 family multiple sequences alignment show a strong conservation of the sucrose hydrolytic machinery among levansucrases and also a structural equivalence of the Bs levanucrase Ca2+-binding site to the LsdA Cys339-Cys395 disulphide bridge, suggesting similar fold-stabilizing roles.
View on PubMed
...
...
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy, Terms of Service, and Dataset License