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- W24062283 endingPage "296" @default.
- W24062283 startingPage "283" @default.
- W24062283 abstract "Proteinases play key roles in many essential physiological processes, and are of great importance in maintaining various cellular functions. With the advent of molecular biology in the 20th Century, remarkable progress has been made in understanding the molecular structure and function, catalytic mechanism, and evolution of proteinases. Further, it has become evident that proteinases can be classified into families, with the members of each family having similar structures and catalytic mechanisms1. In parallel with this, we also have witnessed dramatic advances in understanding the term proteolysis, which is one of the most important enzymatic protein modifications. Careful control of the levels of structural proteins, enzymes, and regulatory proteins is essential to maintain the proper cellular functioning. Generally, structural proteins or proteins that are constitutively required are longlived, whereas regulatory proteins are otten rapidly degraded. Furthermore, their degradation must be precisely timed and regulated, because unregulated degradation would be quite hazardous to cells. Ultimately, the balance between the rate of synthesis and the breakdown of cellular proteins determines the fate of cells in vivo. Thus, the highly complex and regulated mechanism, termed proteolysis, has evolved to accomplish this purpose. As indicated in Table 1, the widely used term protease, which is synonymous to peptidase, can be applied equally to both exopeptidases and endopeptidases. In contrast, the term proteinase is applied only to endopeptidases, and four mechanistic classes of proteinases are recognized by the IUBMB as described below1. This chapter will mainly describe mammalian proteinases possessing endopeptidase activity. However, to describe all mammalian proteinases is beyond the scope of this chapter. It is the aim of this chapter to summarize mammalian proteinases briefly and to explain the structural and evolutionary characteristics of their genes on the basis of recent information." @default.
- W24062283 created "2016-06-24" @default.
- W24062283 creator A5023317571 @default.
- W24062283 creator A5073962937 @default.
- W24062283 creator A5077483738 @default.
- W24062283 date "2005-12-17" @default.
- W24062283 modified "2023-10-10" @default.
- W24062283 title "Mammalian Proteinase Genes" @default.
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- W24062283 doi "https://doi.org/10.1007/0-306-46847-6_18" @default.
- W24062283 hasPublicationYear "2005" @default.
- W24062283 type Work @default.