Degradation of 2-ketoarginine by guanidinobutyrase in arginine aminotransferase pathway of Brevibacterium helvolum.
Guanidinobutyrase (EC 3.5.3.7) involved in the arginine oxygenase pathway of Brevibacterium helvolum IFO 12073 was found to catalyze also the hydrolysis of 2-ketoarginine (2-keto-5-guanidinovalerate) to 2-ketoornithine (2-keto-5-aminovalerate) and urea, the second step of the arginine aminotransferase pathway. No other enzyme that degraded 2-ketoarginine was found in cells grown on L-arginine. The enzyme hydrolyzed 2-ketoarginine with a relative rate of about 0.7% of that toward 4-guanidinobutyrate. The Km for 2-ketoarginine was 33 mM.
Yorifuji
T
T
Department of Bioscience and Biotechnology, Shinshu University, Nagano, Japan.
Kaneoke
M
M
Okazaki
T
T
Shimizu
E
E
D001120:Arginine / Q000031:analogs & derivatives* / Q000302:isolation & purification / Q000378:metabolism; D001951:Brevibacterium / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D007700:Kinetics; D000637:Transaminases / Q000302:isolation & purification / Q000378:metabolism*; D014512:Ureohydrolases / Q000378:metabolism*
C093466:2-ketoarginine; D001120:Arginine; D000637:Transaminases; D014512:Ureohydrolases; C020835:guanidinobutyrase