Dempsey W B, Ito H
J Bacteriol. 1970 Nov;104(2):658-67. doi: 10.1128/jb.104.2.658-667.1970.
At least six phenotypically distinct classes of mutants of Escherichia coli which require serine or pyridoxine or both can be isolated. Three of the six classes lack 3-phosphoserine-2-oxoglutarate aminotransferase. One of these classes contains WG5, a mutant previously characterized as containing the pdxF5 allele. The aminotransferase isolated from this mutant has been compared to that isolated from wild-type E. coli and found to have apparently normal affinity for pyridoxal 5'-phosphate, but reduced affinity for pyridoxamine 5'-phosphate.
至少可以分离出六类表型不同的大肠杆菌突变体,它们需要丝氨酸或吡哆醇或两者都需要。这六类中的三类缺乏3-磷酸丝氨酸-2-氧代戊二酸氨基转移酶。其中一类包含WG5,这是一种先前被鉴定为含有pdxF5等位基因的突变体。已将从该突变体中分离出的氨基转移酶与从野生型大肠杆菌中分离出的氨基转移酶进行了比较,发现它对磷酸吡哆醛5'-磷酸具有明显正常的亲和力,但对磷酸吡哆胺5'-磷酸的亲和力降低。