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 } }
3 Citations
Characterization of an Arginine:Pyruvate Transaminase in Arginine Catabolism of Pseudomonas aeruginosa PAO1
- BiologyJournal of bacteriology
- 2007
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.
- Biology, ChemistryJournal of general microbiology
- 1988
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
- Biology
- 2007
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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