Porphyromonas gingivalis, a pathogen of chronic periodontitis, is an asaccharolytic
microorganism that solely utilizes nutritional amino acids as its energy source and cellular …

Proteolytic enzymes and their homologues have been classified into clans by comparing the
tertiary structures of the peptidase domains, into families by comparing the protein …

Classical enzyme optimization exploits the chemistry confined to the 20 canonical amino
acids encoded by the standard genetic code.'Genetic code engineering'allows the global …

The first structure of tetrameric mammalian acylaminoacyl peptidase, an enzyme that
functions as an upstream regulator of the proteasome through the removal of terminal N …

Cold-active enzymes increase their catalytic efficiency at low-temperature, introducing
structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied …

The alpha/beta‐hydrolases are a family of acid‐base‐nucleophile catalytic triad enzymes
with a common fold, but using a wide variety of substrates, having different pH optima …

The number of enzymes endowed with the capacity to catalyse other reactions than the
main, physiological one, a feature that has been called promiscuity, is increasing at a fast …

Oxidative challenge is an important factor affecting the adaptive strategies of Antarctic fish,
but data on antioxidant defenses in these organisms remain scarce. In this context, a key …

Acylaminoacyl peptidase from Aeropyrum pernix is a homodimer that belongs to the prolyl
oligopeptidase family. The monomer subunit is composed of one hydrolase and one …

Reactive oxygen species (ROS) are constant by-products of aerobic life. In excess, ROS
lead to cytotoxic protein aggregates, which are a hallmark of ageing in animals and linked to …