Hashiguchi K, Kojima H, Sato K, Sano K
Central Research Laboratories, Ajinomoto Co., Inc., Kawasaki, Japan.
Biosci Biotechnol Biochem. 1997 Jan;61(1):105-8. doi: 10.1271/bbb.61.105.
A mutated ilvA gene of Escherichia coli encoding a threonine deaminase that is resistant to feedback inhibition by L-isoleucine was obtained. It was functional in Brevibacterium flavum, and a wild strain of B. flavum into which it was introduced became able to convert exogeneous L-homoserine and L-threonine to L-isoleucine. When it was introduced into a L-threonine-producing B. flavum strain, the transformant accumulated 20 g/liter L-isoleucine from 100 g/liter glucose.
获得了大肠杆菌的一个突变ilvA基因，其编码的苏氨酸脱氨酶对L-异亮氨酸的反馈抑制具有抗性。该基因在黄色短杆菌中具有功能，将其导入黄色短杆菌的野生菌株后，该菌株能够将外源L-高丝氨酸和L-苏氨酸转化为L-异亮氨酸。当将其导入一株产L-苏氨酸的黄色短杆菌菌株时，转化体从100克/升葡萄糖中积累了20克/升L-异亮氨酸。
