Pichia pastoris is an established protein expression host mainly applied for the production of
biopharmaceuticals and industrial enzymes. This methylotrophic yeast is a distinguished …

The mammalian proprotein convertases constitute a family of nine secretory serine
proteases that are related to bacterial subtilisin and yeast kexin. Seven of these (proprotein …

Furin catalyses a simple biochemical reaction—the proteolytic maturation of proprotein
substrates in the secretory pathway. But the simplicity of this reaction belies furin's broad and …

Background Lipases constitute a family of enzymes that hydrolyze triglycerides. They occur
in many organisms and display a wide variety of substrate specificities. In recent years …

Proteases form one of the largest and more important groups of enzymes. They selectively
catalyze the hydrolysis of peptide bonds and can be divided into four major classes …

The purpose of this article is to review essential features of the life cycle of the budding yeast
Saccharomyces cerevisiae as a starting point for learning about S. cerevisiae and its cell …

The use of the methylotrophic yeast, Pichia pastoris, as a cellular host for the expression of
recombinant proteins has become increasing popular in recent times. P. pastoris is easier to …

Many viruses have membrane glycoproteins that are activated at cleavage sites containing
multiple arginine and lysine residues by cellular proteases so far not identified. The …

Specificity of Proteolysis presents a survey and conclusions on the action or proteinases-
enzymes which are cleaving proteins or peptides. The specificity of proteinases which is …

Previous work demonstrated that human furin is a predominantly Golgi membrane-localized
endoprotease that can efficiently process precursor proteins at paired basic residues (-Lys …