Serine proteases as metabolic regulators in yeast

Abstract

Serine proteases are enzymes that break peptidic bonds in proteins, being serinethe nucleophilic amino acid at the enzyme's active site. These proteases arefound ubiquitously in both eukaryotes and prokaryotes. Based on their structure, serine proteases may be classified into two super families: chymotrypsin-like(trypsin-like) or subtilisin-like. This chapter focuses on aspects related to themolecular structure, subcellular localization, mechanism of action, and physiologicalrole, among others, of Kexin, Ynm3p, Prb1p, Ssy5p, Lpx1p, and Pcp1p, the best characterized serine proteases found in yeast, taking as a reference thealmost fully characterized yeast model Saccharomyces cerevisiae. Table 1summarizes the general information about the proteases mentioned above, andsuch general information is illustrated in Fig. 1.