Peptidases and proteases of Escherichia coli and Salmonella typhimurium.
A number of peptidases and proteases have been identified in Escherichia coli. Although their specific physiological roles are often not known, some of them have been shown to be involved in: the maturation of nascent polypeptide chains; the maturation of protein precursors; the signal peptide processing of exported proteins; the degradation of abnormal proteins; the use of small peptides as nutrients; the degradation of colicins; viral morphogenesis; the inactivation of some regulatory proteins for which a limited lifetime is a physiological necessity. Some of these enzymes act in concert to carry out specific functions. At present, twelve peptidases and seventeen proteases have been characterized. The specificity for only a few of them is known. The possible roles and the properties of these enzymes are discussed in this review.
Lazdunski
A M
AM
Laboratoire de Chimie Bactérienne, C.N.R.S., Marseille, France.
D004926:Escherichia coli / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000502:physiology*; D012486:Salmonella typhimurium / Q000201:enzymology*
D010447:Peptide Hydrolases