Function of the arginine oxygenase pathway in utilization of L-arginine-related compounds in Arthrobacter globiformis and Brevibacterium helvolum

Two coryneform bacteria, Arthrobacter globiformis IFO 12137 (ATCC 8010) and Brevibacterium helvolum IFO 12073, which have the arginine oxygenase pathway, could utilize L-ornithine, L-citrulline, and D-arginine. The cells of the bacteria grown on these amino acids contained high levels of guanidinobutyrase and induced levels of the enzymes of the preceding steps of the pathway. 4-Guanidinobutyrate induced guanidinobutyrase but failed to induce the other enzymes, indicating that it was the direct inducer of guanidinobutyrase. These amino acids and L-arginine also induced L-arginine: 2-ketoglutarate aminotransferase. 4-Aminobutyrate was formed on incubation of L-citrulline with L-citrulline-grown cells of A. globiformis in the presence of gabaculine; its amount was about 50% of the L-citrulline degraded. The L-arginine-grown cells produced 4-aminobutyrate and urea from L-arginine in the presence of aminooxyacetate or gabaculine; the amount of 4-aminobutyratewas 80% or more of that of the L-arginine degraded. When the oxygenase pathway was blocked with thioglycolate, the degradation of L-arginine and the formation of urea and 4-aminobutyrate were greatly suppressed. These results indicate that these amino acids are degraded via the arginine oxygenase and the arginine aminotransferase pathways and the major route is the former. Agmatine was degraded in these bacteria and induced agmatine deiminase, carbamoylputrescine hydrolase, putrescine oxidase, and aminobutyraldehyde dehydrogenase. None of the enzymes was induced by L-arginine.