Carbon and nitrogen repression of arginine catabolic enzymes in Bacillus subtilis.
Specific activities of arginase and ornithine aminotransferase, inducible enzymes of arginine catabolism in Bacillus subtilis 168, were examined in cells grown with various carbon and nitrogen sources. Levels of these enzymes were similar in arginine-induced cultures whether glucose or citrate was the carbon source (in contrast to histidase), suggesting that carbon source catabolite repression has only limited effect. In media with combinations of nitrogen sources, glutamine strongly repressed induction of these enzymes by proline or arginine. Ammonium, however, only repressed induction by proline and had no effect on induction by arginine. These effects correlate with generation times in media containing these substances as sole nitrogen sources: growth rates decreased in the order glutamine-arginine-ammonium-proline. Similar phenomena were observed when glutamine or ammonium were added to arginine- or proline-grown cultures, or when arginine or proline were added to glutamine- or ammonium-grown cultures. In the latter cases, an additional feature was apparent, namely a surprisingly long transition between steady-state enzyme levels. The results are compared with those for other bacteria and for eucaryotic microorganisms.
D001119:Arginase / Q000096:biosynthesis*; D001412:Bacillus subtilis / Q000201:enzymology*; D002951:Citrates / Q000378:metabolism; D004790:Enzyme Induction; D004794:Enzyme Repression; D005947:Glucose / Q000378:metabolism; D005971:Glutamates / Q000378:metabolism; D005973:Glutamine / Q000378:metabolism; D007700:Kinetics; D009953:Ornithine-Oxo-Acid Transaminase / Q000096:biosynthesis*; D000644:Quaternary Ammonium Compounds / Q000378:metabolism; D000637:Transaminases / Q000096:biosynthesis*
D002951:Citrates; D005971:Glutamates; D000644:Quaternary Ammonium Compounds; D005973:Glutamine; D000637:Transaminases; D009953:Ornithine-Oxo-Acid Transaminase; D001119:Arginase; D005947:Glucose