Author:
Crawford R L,Hutton S W,Chapman P J
Abstract
Gentisate:oxygen 1,2-oxidoreductase (decyclizing) (EC 1.13.11.4; gentisate 1,2-dioxygenase) from Moraxella osloensis was purified to homogeneity as shown by polyacrylamide gel electrophoresis. The enzyme has a molecular weight of about 154,000 and gives rise to subunits of molecular weight 40,000 in the presence of sodium dodecyl sulfate. Gentisate 1,2-dioxygenase showed broad substrate specificity and attacked a range of halogen- and alkyl-substituted gentisic acids. Maleylpyruvate, the product formed from gentisate, was degraded by cell extracts supplemented with reduced glutathione, but substituted maleylpyruvates were not attacked under these conditions.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference27 articles.
1. Purification and properties of homogentisate oxygenase from Pseudomonas fluorescens;Adachi K.;Biochim. Biophys. Acta,1966
2. Isolation of Acinetobacter from soil and water;Baumann P.;J. Bacteriol,1968
3. 4-Aminosalicylic acid and its derivatives. Part II. The synthesis of 4-amino-2:5- and 4-amino-2:3-dihydroxybenzoic acid;Bhattacharya S. C.;J. Chem. Soc.,1950
4. Chapman P. J. 1972. An outline of reaction sequences used for the bacterial degradation of phenol com- pounds p. 17-55. In Degradation of synthetic organic molecules in the biosphere. Printing and Publishing Office National Academy of Sciences Washington D.C.
5. Oxidation of homogentisic acid by cell-free extracts of a vibrio;Chapman P. J.;J. Gen. Microbiol.,1962
Cited by
122 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