Davis R H
J Bacteriol. 1968 Aug;96(2):389-95. doi: 10.1128/jb.96.2.389-395.1968.
Through the use of a mutant deficient in ornithine-delta-transaminase (OTA), it is shown that this enzyme normally has no obligate or even major biosynthetic role in Neurospora. The pathways of ornithine and proline synthesis proceed wholly independently of each other in OTA-less strains. It is probable that OTA functions as an enzyme of arginine catabolism. With mutants affected in OTA, ornithine transcarbamylase, and the synthesis of ornithine, it was demonstrated that exogenous and endogenous ornithine are utilized in different ways. Exogenous ornithine is destined mainly for catabolism, whereas endogenous ornithine is destined mainly for biosynthesis. It is suggested that this distinction depends upon differences in the intracellular location or origin of the two sources of ornithine.
通过使用鸟氨酸-δ-转氨酶(OTA)缺陷型突变体,研究表明该酶在粗糙脉孢菌中通常没有必需的甚至主要的生物合成作用。在无OTA菌株中,鸟氨酸和脯氨酸的合成途径完全相互独立进行。OTA可能作为精氨酸分解代谢的一种酶发挥作用。利用受OTA、鸟氨酸转氨甲酰酶和鸟氨酸合成影响的突变体,证明外源和内源鸟氨酸的利用方式不同。外源鸟氨酸主要用于分解代谢,而内源鸟氨酸主要用于生物合成。有人认为这种区别取决于两种鸟氨酸来源在细胞内位置或起源的差异。