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The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst.
TLDR
These are the first crystal structures of a thermophilic GE both in an unliganded form and bound to a substrate analogue, thus unravelling the organization of the catalytic triad residues and their neighbours lining the active site.
Glucuronoyl Esterase Screening and Characterization Assays Utilizing Commercially Available Benzyl Glucuronic Acid Ester
TLDR
The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery of different GEs through an extensive screening of heterologous Genomic and Metagenomic expression libraries.
Amide-1,2,3-triazole bioisosterism: the glycogen phosphorylase case
Abstract Per-O-acetylated β- d -glucopyranosyl azide was transformed into an intermediate iminophosphorane by PMe 3 which was then acylated to N -acyl-β- d -glucopyranosylamines. The same azide and
Synthesis of variously coupled conjugates of D-glucose, 1,3,4-oxadiazole, and 1,2,3-triazole for inhibition of glycogen phosphorylase.
TLDR
5-Phenyltetrazole was transformed into 5-ethynyl- as well as 5-chloromethyl-2-(O-perbenzoylated-β-D-glucopyranosyl)-1,3,4-oxadiazoles by acylation with propiolic acid-DCC or chloroacetyl chloride by the Zemplén protocol.
The binding of β-d-glucopyranosyl-thiosemicarbazone derivatives to glycogen phosphorylase: A new class of inhibitors.
TLDR
A group of 15 aromatic aldehyde 4-(β-d-glucopyranosyl)thiosemicarbazones have been synthesized and evaluated as inhibitors of rabbit muscle glycogen phosphorylase b by kinetic studies, revealing that the inhibitors are accommodated at the catalytic site with the glucopyranusyl moiety at approximately the same position as α- d-glue and stabilize the T conformation of the 280s loop.
Synthesis of new glycosyl biuret and urea derivatives as potential glycoenzyme inhibitors.
TLDR
Five new compounds exhibited moderate inhibition against rabbit muscle glycogen phosphorylase b and human salivary alpha-amylase and the O-acyl protecting groups were removed under acid- or base-catalyzed transesterification conditions.
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