Enzymatically active peptide from the adenosine diphosphate-ribosylating toxin of Pseudomonas aeruginosa.
Infect Immun, 1977/6;16(3):832-41.
PMID: 19354
Impact factor: 3.609
Abstract
A nontoxic peptide (molecular weight, 26,000), which is active in catalyzing the adenosine diphosphate (ADP)-ribosylation of elongation factor 2, has been isolated from the culture supernatant of Pseudomonas aeruginosa strain 103 in stationary phase. Like fragment A from diphtheria toxin, the active peptide catalyzed the hydrolysis of nicotinamide adenine dinucleotide as well as the ADP-ribosylation of elongation factor 2 and showed similarities to fragment A in specific activity, kinetic constants, pH optimum, and ionic sensitivity. These results provide strong evidence for a high degree of homology in the structures of their active sites. That the peptide is not identical to fragment A is shown by the fact that it was not neutralized by fragment A-specific antiserum and was different in amino acid composition and pH and thermal labilities. Although definitive evidence is lacking, there are data suggesting that this peptide is a proteolytic fragment from the ADP-ribosylating toxin (exotoxin A; molecular weight, 66,000) produced by the same strain of P. aeruginosa.
MeSH terms
Adenosine Diphosphate Sugars; Cell-Free System; Diphtheria Toxin; Hydrogen-Ion Concentration; Molecular Weight; NAD; Peptide Elongation Factors; Peptides; Pseudomonas aeruginosa; Ribose; Temperature; Toxins, Biological
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