Phenylalanine Biosynthesis in Escherichia coli K-12: Mutants Derepressed for Chorismate Mutase P-Prephenate Dehydratase
Phenylalanine Biosynthesis in Escherichia coli K-12: Mutants Derepressed for Chorismate Mutase P-Prephenate Dehydratase
复制标题
大肠杆菌 K-12 中的苯丙氨酸生物合成：分支酸变位酶 P-预苯酸脱水酶去抑制的突变体
DOI：
10.1128/jb.106.3.784-790.1971
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发表时间：
1971
影响因子：
3.2
通讯作者：
J. Pittard
中科院分区：
文献类型：
--
作者：
S. Im;J. Pittard
分离出突变体，其被去阻遏以合成分支酸酯β-预苯酸酯酶。在这些菌株中，没有参与苯丙氨酸合成的其他酶被去阻遏。这些突变体能够在抑制AB 3259生长的邻氟苯丙氨酸和对氟苯丙氨酸浓度下生长，AB 3259是它们的来源菌株。它们还分泌苯丙氨酸。遗传分析表明，导致这种去阻遏的突变与这种酶的结构基因密切相关（与pheA的共转导频率为95%或更高）。它们出现的基因被命名为pheO，因为该基因具有控制pheA结构基因的操纵基因所预测的所有特性。最后，pheO突变等位基因已被证明在二倍体中是显性的。
Mutants were isolated which are derepressed for the synthesis of chorismate mutase P-prephenate dehydratase. No other enzymes involved in the synthesis of phenylalanine are derepressed in these strains. These mutants are able to grow in concentrations of o- and p-fluorophenylalanine that inhibit the growth of AB3259, the strain from which they were derived. They also excrete phenylalanine. Genetic analysis shows that the mutations causing this derepression are closely linked to the structural gene for this enzyme (cotransduction frequency of 95% or more with pheA). The gene in which they occur has been designated pheO since this gene has all of the properties predicted for an operator gene controlling the pheA structural gene. Finally, the pheO mutant alleles have been shown to be dominant in diploids.