Distribution of Amidinohydrolases among Pseudomonas and Comparative Studies of Some Purified Enzymes by One-dimensional Peptide Mapping

Abstract

The distribution of guanidinoacetate amidinohydrolase (GAH), 3-guanidinopropionate amidinohydrolase (GPH) and 4-guanidinobutyrate amidinohydrolase (GBH) among ten representative strains of fluorescent Pseudomonas was examined. GBH was produced by most of the strains, but GPH was produced by Pseudomonas aeruginosa strains only, and GAH was produced by one of the three P. putida strains and by Pseudomonas sp. ATCC 14676. In most of the GBH-producing bacteria, including Pseudomonas sp. ATCC 14676, GBH was induced by L-arginine as well as by 4-guanidinobutyrate. In contrast, the enzyme was induced exclusively by 4-guanidinobutyrate in two strains of P. aeruginosa and a strain of P.fluorescens. GBH of P. aeruginosa PAO1 was purified to apparent homogeneity and the enzyme protein was compared with the GBH protein from Pseudomonas sp. ATCC 14676 by one-dimensional peptide mapping. The fragmentation patterns from the two proteins, generated by subtilisin BPN', thermolysin, α-chymotrypsin, and Staphylococcus aureus V8 protease, exhibited the obvious structural homology between them. These results indicate that P. aeruginosa lacks one or more of the enzymes which participate in the degradation of L-arginine to 4-guanidinobutyrate in P. putida.