Rahman M, Laverack P D, Clarke P H
J Gen Microbiol. 1980 Feb;116(2):371-80. doi: 10.1099/00221287-116-2-371.
Mutants isolated from Pseudomonas aeruginosa strain PAO1632 (Hut-Ami) were unable to utilize L-arginine or L-ornithine as the carbon source for growth. Arginine deiminase (AD), catabolic ornithine carbamoyltransferase (cOTC) and N2-acetylornithine 5-aminotransferase (ACOAT) were present in the mutants but these enzymes were not induced to higher levels by exogenous L-arginine. One group of mutants could utilize L-ornithine but not L-arginine and in these strains L-arginine induced the synthesis of ACOAT but not AD or cOTC. The mutations of the arginine utilization-negative mutants were all in genes of the same transductional linkage group and mapped in the 45 to 50 min region of the chromosome. Revertants isolated on L-arginine or L-ornithine plates were derepressed for the synthesis of ACOAT. It is suggested that L-arginine is normally catabolized by the wild-type strain via the arginine deiminase pathway and requires a threshold level of ACOAT. The regulatory factors controlling the functioning of the divergent arginine deiminase and arginine carboxylase pathways are discussed.
从铜绿假单胞菌PAO1632菌株（Hut-Ami）分离出的突变体无法利用L-精氨酸或L-鸟氨酸作为生长的碳源。突变体中存在精氨酸脱亚氨酶（AD）、分解代谢鸟氨酸氨甲酰转移酶（cOTC）和N2-乙酰鸟氨酸5-氨基转移酶（ACOAT），但这些酶不会被外源L-精氨酸诱导至更高水平。一组突变体可以利用L-鸟氨酸但不能利用L-精氨酸，在这些菌株中，L-精氨酸诱导ACOAT的合成，但不诱导AD或cOTC的合成。精氨酸利用阴性突变体的突变均位于同一转导连锁群的基因中，并定位在染色体的45至50分钟区域。在L-精氨酸或L-鸟氨酸平板上分离出的回复突变体中，ACOAT的合成去阻遏。提示野生型菌株通常通过精氨酸脱亚氨酶途径分解代谢L-精氨酸，并且需要ACOAT的阈值水平。讨论了控制精氨酸脱亚氨酶和精氨酸羧化酶不同途径功能的调控因子。
