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.
Straganz
Grit
G
Institute of Biotechnology, Technical University Graz, Austria.
Brecker
Lothar
L
Weber
Hans-Jorg
HJ
Steiner
Walter
W
Ribbons
Douglas W
DW
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*
D008667:Metalloproteins; D010422:Pentanones; C008790:acetylacetone; D010105:Oxygenases