Takatsuka Y, Tomita T, Kamio Y
Department of Molecular and Cell Biology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Biosci Biotechnol Biochem. 1999 Oct;63(10):1843-6. doi: 10.1271/bbb.63.1843.
Lysine decarboxylase (LDC, EC 4.1.1.18) from Selenomonas ruminantium has decarboxylating activities towards both L-lysine and L-ornithine with similar K(m) and Vmax. Here, we identified four amino acid residues that confer substrate specificity upon S. ruminantium LDC and that are located in its catalytic domain. We have succeeded in converting S. ruminantium LDC to an enzyme with a preference in decarboxylating activity for L-ornithine when the four-residue of LDC were replaced by the corresponding residues of mouse ornithine decarboxylase (EC 4.1.1.17).
来自反刍月形单胞菌的赖氨酸脱羧酶(LDC,EC 4.1.1.18)对L-赖氨酸和L-鸟氨酸均具有脱羧活性,其米氏常数(K(m))和最大反应速度(Vmax)相似。在此,我们鉴定出四个赋予反刍月形单胞菌LDC底物特异性的氨基酸残基,它们位于其催化结构域中。当LDC的四个残基被小鼠鸟氨酸脱羧酶(EC 4.1.1.17)的相应残基取代时,我们成功地将反刍月形单胞菌LDC转化为一种对L-鸟氨酸脱羧活性具有偏好的酶。