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J. Biochem, 1988, Vol. 103, No. 6 1045-1049
© 1988 Japanese Biochemical Society

research-article

L-Alanine: 4,5-Dioxovalerate Aminotransferase from Pseudomonas riboflavina: Purification and Inactivation by Methylglyoxal1

Hae-ik Rhee, Kousaku Murata2 and Akira Kimura

Research Institute for Food Science, Kyoto University Uji, Kyoto 611

2To whom correspondence should be addressed.

L-Alanine: 4,5-dioxovalerate aminotransferase, which catalyzes transamination between L-alanine and 4,5-dioxovalerate to yield {delta}-aminolevulinate and pyruvate, has been purified from Pseudomonas riboflavina IFO 3140. The enzyme had a molecular weight of 190,000 and consisted of four identical subunits. It was crystallized as pale yellow needles. The enzyme used L-alanine (relative activity 100), ß-alanine (39), and L-ornithine (14) as amino donors. {gamma}-Aminobutyrate (55) and {varepsilon}-aminocaproate (34) were also effective as amino donors. The reaction proceeded according to a ping-pong mechanism and the Km values for L-alanine and 4,5-dioxovalerate were 1.7 and 0.75 mM, respectively. The activity of the enzyme is strongly inhibited by pyruvate, hemin, and methylglyoxal. Methylglyoxal interacted with the enzyme and brought about a complete inactivation.

1This work was supported in part by a Grant-in-Aid for Scientific Research (No. 61560120) for K.M. from the Ministry of Education, Science and Culture of Japan.


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