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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Purification and properties of gentisate 1,2-dioxygenase from Moraxella osloensis.

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.[1]

References

  1. Purification and properties of gentisate 1,2-dioxygenase from Moraxella osloensis. Crawford, R.L., Hutton, S.W., Chapman, P.J. J. Bacteriol. (1975) [Pubmed]
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