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Serine Proteases as Metabolic Regulators in Yeast

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Pathophysiological Aspects of Proteases

Abstract

Serine proteases are enzymes that break peptidic bonds in proteins, being serine the nucleophilic amino acid at the enzyme’s active site. These proteases are found 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 the molecular structure, subcellular localization, mechanism of action, and physiological role, among others, of Kexin, Ynm3p, Prb1p, Ssy5p, Lpx1p, and Pcp1p, the best characterized serine proteases found in yeast, taking as a reference the almost fully characterized yeast model Saccharomyces cerevisiae. Table 1 summarizes the general information about the proteases mentioned above, and such general information is illustrated in Fig. 1.

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  1. Departmento de Biología Molecular, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Univesidad Nacional de Río Cuarto, Río Cuarto, Argentina

    Alexis N. Campetelli & Noelia E. Monesterolo

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  1. Alexis N. Campetelli
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  2. Noelia E. Monesterolo
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Correspondence to Alexis N. Campetelli .

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  1. Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, West Bengal, India

    Sajal Chakraborti

  2. Institute of Cardiovascular Sciences, University of Manitoba, Manitoba, Canada

    Naranjan S. Dhalla

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Campetelli, A.N., Monesterolo, N.E. (2017). Serine Proteases as Metabolic Regulators in Yeast. In: Chakraborti, S., Dhalla, N. (eds) Pathophysiological Aspects of Proteases. Springer, Singapore. https://doi.org/10.1007/978-981-10-6141-7_17

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