Henderson G B, Snell E E
Proc Natl Acad Sci U S A. 1971 Dec;68(12):2903-7. doi: 10.1073/pnas.68.12.2903.
A mutant of Salmonella typhimurium LT-2 that requires either vitamin B(6) or histidine for growth was found to synthesize vitamin B(5) in amounts comparable to the parent strain, but to be deficient in imidazoleacetol phosphate transaminase (L-histidinolphosphate: 2-oxoglutarate aminotransferase, EC 2.6.1.9), an enzyme required for histidine biosynthesis. The mutant apotransaminase required a 50-fold higher concentration of pyridoxal 5'-phosphate for half-maximum activation than the corresponding wild-type enzyme; the fully activated mutant enzyme also displays a much lower maximum rate of catalysis than the enzyme from the parent strain. Such mutational changes in bacteria resemble those in certain vitamin B(6)-responsive genetic diseases in man and provide useful experimental material for the study of factors involved in coenzyme binding and enzymatic catalysis.
一株鼠伤寒沙门氏菌LT-2突变体,其生长需要维生素B6或组氨酸,发现该突变体合成维生素B5的量与亲本菌株相当,但缺乏组氨酸生物合成所需的咪唑乙酰磷酸转氨酶(L-组氨酸磷酸:2-氧代戊二酸转氨酶,EC 2.6.1.9)。与相应的野生型酶相比,突变体脱辅基转氨酶达到最大激活一半时所需的磷酸吡哆醛5'-磷酸浓度高50倍;完全激活的突变体酶的最大催化速率也比亲本菌株的酶低得多。细菌中的这种突变变化类似于人类某些维生素B6反应性遗传疾病中的变化,并为研究辅酶结合和酶催化所涉及的因素提供了有用的实验材料。