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J. Biochem, 1989, Vol. 106, No. 1 76-80
© 1989 Japanese Biochemical Society

research-article

Activation of L-Lysine {varepsilon}-Dehydrogenase from Agrobacterium tumefaciens by Several Amino Acids and Monocarboxylates

Hiroyuki Hashimoto, Haruo Misono1, Shinji Nagata and Susumu Nagasaki

Department of Agricultural Chemistry, Kochi University Nankoku, Kochi 783

1To whom correspondence should be addressed.

The activation of lysine {varepsilon} -dehydrogenase [EC 1.4.1. ] by L-lysine was dependent on lysine concentration and was accompanied by association of the dimeric enzymes to a tetramer. The lysine concentration required for the half-maximal activation was 0.28 mM, which was lower than the Km value for L-lysine. In addition to L-lysine, several compounds, which were neither substrates nor inhibitors, activated the enzyme. The compounds which activated the enzyme have common structural characteristics: they have both a carboxyl group and a hydrophobic side chain. These activators also induced the association of the enzyme. The activation of the enzyme occurred well over the pH range 5.0 to 7.5, and the maximal activation was obtained by preincubation for 5 min at 30°C and pH 7.4, when 5 mM L-lysine or 6-aminocaproate was used as an activator. NADH binding experiments indicated that about 2 mol of NADH bind to 1 mol of the tetrameric enzyme: the dimeric enzyme has one catalytic site. Binding experiments with n-[l-14C]heptanoate and L-[U-14C]lysine showed that approximately 2 mol of ligands bind to 1 mol of the dimeric enzyme and L-lysine could not bind to the catalytic site of the enzyme in the absence of NAD+. These results indicate the presence of one catalytic site and two activator binding sites in the dimeric enzyme.


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