Chemical and immunological properties of B. anthracis arginase and its metabolic involvement

Abstract

An arginase isolated from a capsulated Bacillus anthracis strain was highly purified and crystallized. The chemical and immunological characteristics of this enzyme are described. Some very important properties differ from those of another bacterial arginase, i.e. Staphylococcus aureus arginase, described in a previous paper (Soru et al. (2)). The two arginases have different crystallization forms, different molecular weight, Km, thermostability, Arrhenius activation energy. They have another N-terminal group and are immunologically strictly specific. These differences point to distinct proteins. The fact that two arginases of different origin are structurally non-identical suggests that they may be involved in different metabolic processes. Staphylococcal arginase was shown to participate in a complete ureogenetic cycle, for it also possesses the other enzymes of the cycle (Soru et al. (2)). Except arginase, no other enzyme of this cycle was identified in the capsulated B. anthracis strain. Arginase may be involved in another metabolic pathway, one that is important for the strain, such as the synthesis of glutamic acid, since the capsular material of the strain is a polymer gamma-linked polyglutamic acid, mainly configuration D (Ivanovic and Bruckner (20)). The fact that the N-terminal residue of B. anthracis arginase is a tetramer containing glutamic acid together with proline (in addition to alanine and glycine) suggests that arginase may participate as a regulatory enzyme in the synthesis of glutamic acid from proline via ornithine and arginine, respectively. This pathway is found in many bacteria. The proline oxidase system, which is supposed to catalyse the conversion of proline to glutamic acid, is under study now in Bacillus anthracis strains.