The structure of putative N-acetyl glutamate kinase from Thermus thermophilus reveals an intermediate active site conformation of the enzyme.

@article{Sundaresan2012TheSO,
  title={The structure of putative N-acetyl glutamate kinase from Thermus thermophilus reveals an intermediate active site conformation of the enzyme.},
  author={Ramya Sundaresan and Preethi T. Ragunathan and Seiki Kuramitsu and Shigeyuki Yokoyama and Thirumananseri Kumarevel and Karthe Ponnuraj},
  journal={Biochemical and biophysical research communications},
  year={2012},
  volume={420 3},
  pages={
          692-7
        }
}
The de novo biosynthesis of arginine in microorganisms and plants is accomplished via several enzymatic steps. The enzyme N-acetyl glutamate kinase (NAGK) catalyzes the phosphorylation of the γ-COO(-) group of N-acetyl-L-glutamate (NAG) by adenosine triphosphate (ATP) which is the second rate limiting step in arginine biosynthesis pathway. Here we report the crystal structure of putative N-acetyl glutamate kinase (NAGK) from Thermus thermophilus HB8 (TtNAGK) determined at 1.92Å resolution. The… CONTINUE READING
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