Distribution of the Arginine Oxygenase Pathway among Coryneform Bacteria

Abstract

Of 14 coryneform and 2 Micrococcus strains tested, Arthrobacter globiformis IFO 12137, A. simplex IFO 12069, and Brevibacterium helvolum IFO 12073 utilized L-arginine as a sole carbon and nitrogen source, and synthesized the enzymes specific for the arginine oxygenase pathway when grown on L-arginine. The first step reaction was stimulated by FAD and aeration, and the enzyme responsible was shown to be arginine 2-monooxygenase (EC 1.13.12.1). High activities of five enzymes, including guanidinobutyramidase and ganidinobutyrase (EC 3.5.3.7), were detected in the extract of L-argininegrown A. simplex cells. The enzymes in the last two steps, 4-aminobutyrate aminotransferase (EC 2.6.1.19) and succinate-semialdehyde dehydrogenase (EC 1.2.1.16), of B. helvolum were also induced by putrescine. These results indicate that some bacteria belonging to the coryneform group employ the arginine oxygenase pathway as a major route for L-arginine metabolism, L-arginine being degraded to succinate via 4-guanidinobutyramide and 4-guanidinobutyrate. The last part of the pathway may be common to the pathway for putrescine degradation.