Existence, localization and regulation of the biosynthesis of aminoendopeptidase in gram-negative bacteria.
An enzyme capable of hydrolyzing the substrate L-alanine p-nitroanilide has been found in 18 gram-negative Enterobacteriaceae and Pseudomonas that we tested. This enzyme might be located near the cell surface. Contrastingly we have not detected this activity on colonies of the 8 gram-positive Bacillus that we tested, which suggest a taxonomic value for this test. The aminoendopeptidases found in the various gram-negative bacteria showed similar electrophoretic mobilities and immunological cross-reactivity when tested again Escherichia coli anti-aminoendopeptidase antiserum. The regulation of aminoendopeptidase biosynthesis by the endogenous level of inorganic phosphate that we previously demonstrated in E. coli has been found to exist in all gram-negative organisms tested.
D000409:Alanine / Q000031:analogs & derivatives; D000626:Aminopeptidases / Q000096:biosynthesis / Q000276:immunology; D001407:Bacillus / Q000201:enzymology; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000096:biosynthesis / Q000276:immunology; D004755:Enterobacteriaceae / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D010710:Phosphates / Q000494:pharmacology; D011549:Pseudomonas / Q000201:enzymology*
D010710:Phosphates; D010450:Endopeptidases; D000626:Aminopeptidases; D000409:Alanine