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Literature summary extracted from

  • Haruyama, K.; Nakai, T.; Miyahara, I.; Hirotsu, K.; Mizuguchi, H.; Hayashi, H.; Kagamiyama, H.
    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 (2001), Biochemistry, 40, 4633-4644.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.9 native and complexed with L-histidinol phosphate or N-(5'-phosphopyridoxyl)-L-glutamate, hanging drop vapor diffusion method Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.9 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate Escherichia coli histidine pathway L-histidinol phosphate + 2-oxoglutarate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.9 Escherichia coli P06986
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.9 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate histidine pathway Escherichia coli L-histidinol phosphate + 2-oxoglutarate
-
 ?
2.6.1.9 L-histidinol phosphate + 2-oxoglutarate
-
 Escherichia coli 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-Glu i.e. imidazoleacetol phosphate + L-Glu ?

Subunits

EC Number Subunits Comment Organism
2.6.1.9 dimer homodimer, crystallization experiments Escherichia coli