The diversity of oligo-and polysaccharides provides an abundance of biological roles for
these carbohydrates. The enzymes hydrolysing these compounds, the glycoside hydrolases …

For technical, environmental and economical reasons, industrial demands for process-fitted
enzymes have evolved drastically in the last decade. Therefore, continuous efforts are made …

The new empirical rules for protein p K a predictions implemented in the PROPKA3. 0
software package (Olsson et al. J. Chem. Theory Comput. 2010, 7, 525–537) have been …

In order to accelerate the hydrolysis of glycosidic bonds by factors approaching 1017-fold,
glycosidases have evolved finely tuned active sites optimally configured for transition-state …

Humans host an intestinal population of microbes—collectively referred to as the gut
microbiome—which encode the carbohydrate active enzymes, or CAZymes, that are absent …

In protein and RNA macromolecules, only a limited number of different side‐chain chemical
groups are available to function as catalysts. The myriad of enzyme‐catalyzed reactions …

The chitinolytic machinery of S erratia marcescens is one of the best known enzyme systems
for the conversion of insoluble polysaccharides. This machinery includes four chitin‐active …

Profitable biomass conversion processes are highly dependent on the use of efficient
enzymes for lignocellulose degradation. Among the cellulose degrading enzymes, beta …

The p K a values and charge states of ionizable residues in polypeptides and proteins are
frequently determined via NMR-monitored pH titrations. To aid the interpretation of the …

Abstract Not “from above”, but “from the side”: Configuration‐retaining β‐glycosidases
protonate their substrate either anti or syn to the endocyclic C1− O bond as the first step in …