Abstract
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.
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