Schrell A, Alt-Moerbe J, Lanz T, Schroeder J
Institut für Biologie II, Universität Freiburg, FRG.
Eur J Biochem. 1989 Oct 1;184(3):635-41. doi: 10.1111/j.1432-1033.1989.tb15060.x.
Agrobacterium nopaline Ti plasmids code for three enzymes of nopaline [N2-(1,3-dicarboxypropyl)-L-arginine] degradation: nopaline oxidase, arginase, and ornithine cyclodeaminase. We describe the DNA sequence of the arginase gene, a comparison of the deduced protein sequence with eucaryotic arginases, and properties of the procaryotic enzyme. The results show that the agrobacterial arginase is related with arginases from yeast, rat liver, and human liver (28-33% identity). The Ti plasmid enzyme revealed several properties which appear common to all arginases, but it does not utilize L-canavanine as substrate, and its Mn2+ requirement is not satisfied by Fe2+, Co2+, or Ni2+. The properties of arginase and ornithine cyclodeaminase are discussed as part of the mechanisms which avoid depletion of L-arginine and L-ornithine pools for biosynthetic reactions during catabolic utilization of nopaline.
根癌农杆菌胭脂碱Ti质粒编码三种参与胭脂碱[N2-(1,3-二羧丙基)-L-精氨酸]降解的酶：胭脂碱氧化酶、精氨酸酶和鸟氨酸环脱氨酶。我们描述了精氨酸酶基因的DNA序列，将推导的蛋白质序列与真核精氨酸酶进行了比较，并研究了原核酶的特性。结果表明，农杆菌精氨酸酶与酵母、大鼠肝脏和人类肝脏中的精氨酸酶相关（同一性为28-33%）。Ti质粒酶显示出一些所有精氨酸酶共有的特性，但它不利用L-刀豆氨酸作为底物，并且其对Mn2+的需求不能被Fe2+、Co2+或Ni2+满足。作为在胭脂碱分解代谢利用过程中避免生物合成反应中L-精氨酸和L-鸟氨酸库耗尽的机制的一部分，讨论了精氨酸酶和鸟氨酸环脱氨酶的特性。
