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

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A novel beta-diketone-cleaving enzyme from Acinetobacter johnsonii: acetylacetone 2,3-oxygenase.

A novel Fe+Zn containing oxygenase from Acinetobacter johnsonii catalyses 2,3-cleavage of acetylacetone to acetate and methylglyoxal has been purified. The stoichiometry of reactants and products conforms to a classical dioxygenase. The pure protein is a homotetramer of 64kD with variable amounts of Fe(2+) and Zn(2+). Activity of the enzyme is more closely related to the Fe(2+) content than to the amount of protein. A purification of acetylacetone 2,3-oxygenase, some of its physical properties, and the preference for some analogous substrates are described.[1]

References

  1. A novel beta-diketone-cleaving enzyme from Acinetobacter johnsonii: acetylacetone 2,3-oxygenase. Straganz, G., Brecker, L., Weber, H.J., Steiner, W., Ribbons, D.W. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
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