Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme.

@article{Haruyama2001StructuresOE,
  title={Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme.},
  author={Kunio Haruyama and Takahisa Nakai and Ikuko Miyahara and Ken Hirotsu and Hiroyuki Mizuguchi and Hideyuki Hayashi and Hiroyuki Kagamiyama},
  journal={Biochemistry},
  year={2001},
  volume={40 15},
  pages={4633-44}
}
Histidinol-phosphate aminotransferase (HspAT) is a key enzyme on the histidine biosynthetic pathway. HspAT catalyzes the transfer of the amino group of L-histidinol phosphate (Hsp) to 2-oxoglutarate to form imidazole acetol phosphate (IAP) and glutamate. Thus, HspAT recognizes two kinds of substrates, Hsp and glutamate (double substrate recognition). The crystal structures of native HspAT and its complexes with Hsp and N-(5'-phosphopyridoxyl)-L-glutamate have been solved and refined to R… CONTINUE READING

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