Open AccessEnzymatic activities for interconversion of purines in spirochetes
Author(s) -
E. Canale-Parola,
George W. Kidder
Publication year - 1982
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.152.3.1105-1110.1982
Subject(s) - purine nucleoside phosphorylase , biology , biochemistry , adenosine deaminase , purine , inosine , guanosine , purine metabolism , hypoxanthine , enzyme , amp deaminase , guanine , nucleoside , adenine phosphoribosyltransferase , nucleotide , adenosine , phosphoribosyltransferase , treponema denticola , nucleic acid , hypoxanthine guanine phosphoribosyltransferase , bacteria , mutant , gene , genetics , porphyromonas gingivalis
Enzymatic activities that catalyze the interconversion of purines and purine derivatives were detected in cell extracts of Spirochaeta aurantia, Spirochaeta stenostrepta, Treponema succinifaciens, and Treponema denticola. Phosphoribosyltransferase activities present in cell extracts of each of the four spirochete species functioned in the conversion of adenine, hypoxanthine, and guanine to AMP, IMP, and GMP, respectively. Nucleotidase activities in the extracts mediated the formation of nucleosides from nucleotides. The conversion of adenosine, inosine, and guanosine to the respective purine bases was catalyzed by nucleoside phosphorylase and, in some instances, by nucleoside hydrolase activities. Guanine deaminase activity was found in both S. aurantia and S. stenostrepta, whereas adenosine deaminase activity was detected only in S. aurantia. Adenine deaminase activity in T. succinifaciens extracts was sensitive to O2 and was relatively resistant to heating. Our results indicate that the four species of spirochetes studied possess a broad spectrum of purine interconversion enzymes. It is suggested that these enzymes may function in metabolic processes important for the survival of spirochetes in nutrient-poor natural environments.