Toshio Kakimoto

Crystallization of L-arginine deiminase from Pseudomonas Putida.

L-Arginine deiminase (EC 3 5.3.6) catalyzes the degradation of L-arginine to L-citrulline and ammonia. Many reports have appeared on the occurrence of this enzyme, but there are only two reports on the exhaustive purification of the enzyme [ 1,2] . As reported in our previous report [3] , we found that Pseudomonas putida produced markedly high activity of L-arginine deiminase and the enzyme is useful for the production of L-citrulline from L-arginine This report describes the crystallization of Larginine deiminase of P. putida.

Subunit and amino acid composition of L-arginine deiminase of Pseudomonas putida.

The preparation and some enzymatic properties of crystalline L-arginine deiminase (L-arginine iminohydrolase, EC 3.5.3.6) of Pseudomonas putida have been described [ 1,2] . The properties of this enzyme are different from those of Streptococcus enzyme [3] in inhibition by carbonyl reagents, and from those of Mycoplasma hominis [4] and Mycoplasma arthritidis [S] in molecular size. This paper describes the subunit structure, and amino acid composition of L-arginine deiminase of Ps. putida. It also describes the identification of the aminoand carboxyl-terminal amino acids of this enzyme, and quantitation of these residues.