title: A novel beta-diketone-cleaving enzyme from Acinetobacter johnsonii: acetylacetone 2,3-oxygenase.
abstract: 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.
authors.affiliation: Institute of Biotechnology, Technical University Graz, Austria.
authors.forename: Grit
authors.initials: G
authors.lastname: Straganz
authors.forename: Lothar
authors.initials: L
authors.lastname: Brecker
authors.forename: Hans-Jorg
authors.initials: HJ
authors.lastname: Weber
authors.forename: Walter
authors.initials: W
authors.lastname: Steiner
authors.forename: Douglas W
authors.initials: DW
authors.lastname: Ribbons
mesh_terms: D000150:Acinetobacter / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D008667:Metalloproteins / Q000737:chemistry / Q000378:metabolism; D015394:Molecular Structure; D010105:Oxygenases / Q000737:chemistry / Q000378:metabolism*; D010422:Pentanones / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008667:Metalloproteins; D010422:Pentanones; C008790:acetylacetone; D010105:Oxygenases