Degradation of 2-ketoarginine by guanidinobutyrase in arginine aminotransferase pathway of Brevibacterium helvolum.

Article abstract of DOI:10.1271/bbb.59.512

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.

Full text of DOI:10.1271/bbb.59.512

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Degradation of 2-Ketoarginine by Guanidinobutyrase
in Arginine Aminotransferase Pathway of
Brevibacterium helvolum
a
a
a
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Takamitsu Yorifuji , Mitsuoki Kaneoke , Takao Okazaki & Eiichi Shimizu
a
Department of Bioscience and Biotechnology, Shinshu University, Minamiminowa,
Nagano 399–45, Japan
Published online: 12 Jun 2014.
To cite this article: Takamitsu Yorifuji, Mitsuoki Kaneoke, Takao Okazaki & Eiichi Shimizu (1995) Degradation of 2-
Ketoarginine by Guanidinobutyrase in Arginine Aminotransferase Pathway of Brevibacterium helvolum, Bioscience,
Biotechnology, and Biochemistry, 59:3, 512-513, DOI: 10.1271/bbb.59.512
To link to this article: http://dx.doi.org/10.1271/bbb.59.512
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