Kimura K, Goto T
J Biochem. 1977 May;81(5):1367-73.
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. subtilis. The molecular weights of the reductases of B. cereus and B. megaterium were fount 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 micrometer and 62 micrometer, respectively, with B. cereus reductase, and 13 micrometer and 59 micrometer 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 Ki values were 85 micrometer and 140 micrometer, 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.
从蜡状芽孢杆菌和巨大芽孢杆菌的粗提物中纯化出了比原来纯度高100倍的二氢二吡啶甲酸还原酶，并将它们的性质与枯草芽孢杆菌的还原酶进行了比较。蜡状芽孢杆菌和巨大芽孢杆菌还原酶的分子量分别为155,000和150,000。与含有黄素的枯草芽孢杆菌酶不同，这些还原酶被证明不含黄素。NADPH和NADH均可作为这两种还原酶的辅酶。NADPH的效果比NADH高三到四倍。蜡状芽孢杆菌还原酶对NADPH和二氢二吡啶甲酸的Km值分别为8微摩尔和62微摩尔，巨大芽孢杆菌还原酶的Km值分别为13微摩尔和59微摩尔。蜡状芽孢杆菌和巨大芽孢杆菌酶的最适pH分别为pH 7.4和7.2。二吡啶甲酸盐对还原酶的抑制作用相对于二氢二吡啶甲酸盐是非竞争性的，其Ki值分别为85微摩尔和140微摩尔。赖氨酸和二氨基庚二酸没有抑制作用。蜡状芽孢杆菌和巨大芽孢杆菌还原酶的性质相似，但与枯草芽孢杆菌的酶有很大不同。然而，与大肠杆菌的酶不同，所有三种芽孢杆菌还原酶都受到二吡啶甲酸盐的显著抑制。
