Purification, properties and formation of arginine-alpha-ketoglutarate transaminase in Arthrobacter simplex.

@article{Tachiki1980PurificationPA,
  title={Purification, properties and formation of arginine-alpha-ketoglutarate transaminase in Arthrobacter simplex.},
  author={Takashi Tachiki and Hirao Kohno and K Sugiyama and T Matsubara and Tatsurokuro Tochikura},
  journal={Biochimica et biophysica acta},
  year={1980},
  volume={615 1},
  pages={
          79-84
        }
}
Characterization of an Arginine:Pyruvate Transaminase in Arginine Catabolism of Pseudomonas aeruginosa PAO1
TLDR
Results implied that AruH may have a broader physiological function in amino acid catabolism, as it has a novel substrate specificity with an order of preference of Arg > Lys > Met > Leu > Orn > Gln.
The fourth arginine catabolic pathway of Pseudomonas aeruginosa.
TLDR
The existence of four arginine catabolic pathways illustrates the metabolic versatility of P. aeruginosa and indicates that the kauB locus was mapped on the chromosome between lysA and argB and was not linked to known genes involved in the three L-arginineCatabolic pathways.
Functional Characterization of the Arginine Transaminase Pathway in Pseudomonas aeruginosa PAO1
TLDR
The arginine transaminase (ATA) pathway is proposed that removes the α-amino group of L-arginine via transamination instead of oxidative deamination by dehydrogenase or oxidase as originally proposed.

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Degradation of Arginine via α-Keto-δ-Guanidinovalerate and α-Keto-δ-Aminovalerate in Arginine-Grown Arthrobacter simplex
TLDR
The results indicated the transamination of arginine-α-ketoglutarate (α-KGA) and the hydrolyzing reaction of ketoarginine into α-keto-δ-aminovalerate and urea.
Separation of L-Leucine-pyruvate and L-Leucine-α-ketoglutarate Transaminases in Acetobacter suboxydans and Identification of Their Reaction Products
l-Leucine-pyruvate and l-leucine-α-ketoglutarate(α-KGA) transaminases were separated by DEAE-cellulose column chromatography and partially purified to 200- and 50-fold, respectively, from the