Abstract
Growth on phenol of two strains of Pseudomonas putida biotype A, NCIB 10015 and NCIB 9865, elicits the synthesis of an enzyme that hydrolyzes 2-hydroxy-6-oxo-2,4-heptadienoate to 2-oxopent-4-enoate. The purified enzyme from Pseudomonas NCIB 10015 has a molecular weight of 118,000 and dissociates in sodium dodecyl sulfate to a species of molecular weight 27,700; the enzyme from Pseudomonas NCIB 9865 has a molecular weight of 100,000 and dissociates to a species of 25,000 molecular weight. The hydrolases from both strains have similar Km values, pH optima, and thermal labilities and attack the same range of substrates. Neither hydrolase was stimulated by Mg2+ or Mn2+, and both were inhibited by p-chloromercuribenzoate and iodoacetamide. Immunodiffusion studies with the purified enzymes and antibodies formed against them show some cross-reaction of Pseudomonas NCIB 9865 enzymes with antibodies to Pseudomonas NCIB 10015, but not vice versa.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference26 articles.
1. Determination of molecular weight of proteins;Andrews P.;Biochem. J.,1964
2. Oxoenoic acids as metabolites in the bacterial degradation of catechols;Bayly R. C.;Biochem. J.,1969
3. The metabolism of cresols by species of Pseudomonas;Bayly R. C.;Biochem. J.,1966
4. Metabolism of phenol and cresols by mutants of Pseudomonasputida;Bayly R. C.;J. Bacteriol.,1973
5. Chapman P. J. 1972. An outline of reaction sequences used for the bacterial degradation of phenolic compounds p. 17-5. In Degradation of synthetic organic molecules in the biosphere. National Academy of Sciences Washington D.C.
Cited by
28 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献