Species: Pimelobacter simplex
Subunit composition of arginine-α-ketoglutarate transaminase = [arginine-α-ketoglutarate transaminase subunit]
arginine-α-ketoglutarate transaminase was purified from Pimelobacter simplex grown on L-arginine as a carbon source. Synthesis of the enzyme was inducible by either L-arginine or 5-guanidino-2-oxo-pentanoate. Catabolite repression of enzyme formation was observed upon addtion of β-D-glucopyranose or glycerol to the media.
The enzyme required a pyridoxal 5'-phosphate cofactor, and demonstrated activity with alternative substrates. Activity with N-nitro-L-arginine, L-citrulline and L-alanine was 22.5, 15.8 and 9.5% of the activity with L-arginine, respectively. The enzyme could also use pyruvate instead of 2-oxoglutarate, with 12% of the activity [Tachiki80].
Molecular Weight of Multimer: 110 kD (experimental) [Tachiki80]
Enzymatic reaction of: arginine-α-ketoglutarate transaminase
EC Number: 2.6.1.-L-arginine + 2-oxoglutarate ⇄ L-glutamate + 5-guanidino-2-oxo-pentanoate
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.
This reaction is reversible.Alternative Substrates for 2-oxoglutarate: pyruvate [Tachiki80]
In Pathways: L-arginine degradation XIHg2+ [Tachiki80], phenylhydrazine [Tachiki80], p-chloromercuribenzoate [Tachiki80]Kinetic Parameters:
pH(opt): 8-8.5 [Tachiki80]
Tachiki80: Tachiki T, Kohno H, Sugiyama K, Matsubara T, Tochikura T (1980). "Purification, properties and formation of arginine-alpha-ketoglutarate transaminase in Arthrobacter simplex." Biochim Biophys Acta 615(1);79-84. PMID: 7426667
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