Purification and properties of gentisate 1,2-dioxygenase from Moraxella osloensis.
R L Crawford, S W Hutton, P J Chapman
Index: J. Bacteriol. 121(3) , 794-9, (1975)
Full Text: HTML
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.
Related Compounds
Related Articles:
2015-06-26
[J. Biol. Chem. 290 , 15949-60, (2015)]
Effect of intramolecular hydrogen bonding on the relative acidities of substituted salicylic acids in benzene solution. Dunn GE and Penner TL.
[Can. J. Chem. 45(14) , 1699-1706, (1967)]
Fluorosalicylohydroxamic acids. Ostaszynski A, et al.
[Bull. Acad. Polon. Sci. Ser. Sci. Chim. 8 , 591-597, (1960)]