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- W1588162399 abstract "Abstract The peptidases present in Escherichia coli K-12 that can cleave lysine oligopeptides were characterized to establish a system in which one could examine questions relating to peptidase specificity, function, and regulation. As an aid to this study, a mutant with diminished peptidase activity was isolated with the use of the reduced ability to cleave trilysine as a screening procedure. In this simplified system, the remaining enzymatic capacity to cleave lysine homopeptides was then characterized. On the basis of substrate specificities and cofactor requirements as well as resolution of the enzymes by ion exchange and Sephadex chromatography; it was shown that the mutant contains the following lysine peptidases: (a) a Co++-dependent peptidase capable of splitting dilysine, (b) an EDTA-sensitive peptidase specific for trilysine, and (c) an endopeptidase that can cleave tetralysine but has no activity toward di- or trilysine. The parental K-12 strain contains, in addition to these three activities, a metal-independent peptidase capable of cleaving all three lysine peptides." @default.
- W1588162399 created "2016-06-24" @default.
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- W1588162399 date "1970-12-01" @default.
- W1588162399 modified "2023-09-27" @default.
- W1588162399 title "Peptidases in Escherichia coli K-12 Capable of Cleaving Lysine Homopeptides" @default.
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- W1588162399 doi "https://doi.org/10.1016/s0021-9258(18)62564-5" @default.
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