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- W1571857100 abstract "Publisher Summary This chapter describes the isolation and assay of protease La from Escherichia coli and summarizes some of its enzymatic properties. Adenosine triphosphate (ATP)-dependent cytosolic protease La is product of the lon gene and plays an important role in intracellular protein degradation. Protease La serves as a paradigm for other ATP-dependent proteases from prokaryotic and eukaryotic cells, all of which use the energy of ATP hydrolysis to accelerate the rate-limiting steps in the kinetically driven degradation of proteins. This enzyme catalyzes the rate-limiting steps in the degradation of highly abnormal proteins in E. coli and certain short-lived regulatory proteins. This enzyme has ATPase and proteolytic activity and is a multimeric structure of high molecular mass. Protease La also has multiple modes of interaction with proteins such that the proteolytic active site remains in an inactive state until an appropriate substrate binds to an allosteric site on the enzyme. This binding step temporarily activates the enzyme and leads to rapid degradation of the bound protein. Enzymes closely homologous to protease La (Lon protease) appear to be widespread in nature." @default.
- W1571857100 created "2016-06-24" @default.
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- W1571857100 date "1994-01-01" @default.
- W1571857100 modified "2023-09-23" @default.
- W1571857100 title "[25] ATP-dependent protease La (Lon) from Escherichia coli" @default.
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- W1571857100 doi "https://doi.org/10.1016/0076-6879(94)44027-1" @default.
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