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J. Biochem, 1977, Vol. 81, No. 5 1367-1373
© 1977 Japanese Biochemical Society

research-article

Dihydrodipicolinate Reductases from Bacillus cereus and Bacillus megaterium

Kinuko KIMURA and Tetsuhisa GOTO1

Laboratory of Biochemistry, College of Science, St Paul's (Rikkyo) University Nishi-Ikebukuro, Toshima-ku, Tokyo 171

Dyhydrodipicolinate reductases were purified 100-fold from crude extracts of B. cereus and B. megaterium and their properties were compared with those of the reductase from B. sub-tilis. The molecular weights of the reductases of B. cereus and B. megaterium were found to be 155,000 and 150,000, respectively. These reductases were shown to be free of flavin, unlike the B. subtilis enzyme, which contains flavin. Both NADPH and NADH acted as coenzymes for these two reductases, NADPH being three or four times more effective than NADH. The Km values for NADPH and dihydrodipicolinate were 8 µM and 62 µM, respectively, with B. cereus reductase, and 13 µM and 59 µM with B. megaterium reductase. The pH optima of the enzymes from B. cereus and B. megaterium were pH 7.4 and 7.2, respectively. The reductases were inhibited by dipicolinate noncompetitively with respect to dihydrodipicolinate and the K1 values were 85 µM and 140 µM, respectively. Lysine and diaminopimelate were not inhibitory. The properties of the reductases from B. cereus and B. megaterium were similar, but they differed considerably from those of the B. subtilis enzyme. However, all three Bacillus reductases were markedly inhibited by dipicolinate, unlike the enzyme from E. coli.

1Present address Mycotoxin Laboratory, National Food Research Institute, Ministry of Agriculture and Forestry, Shiohama, Koto-ku, Tokyo 135.


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