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Gene Review

hisC  -  histidinol-phosphate aminotransferase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2016, JW2003
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Disease relevance of hisC


High impact information on hisC


Biological context of hisC

  • The complete nucleotide sequence of the hisC gene has been determined [1].
  • The crystal structures of native HspAT and its complexes with Hsp and N-(5'-phosphopyridoxyl)-L-glutamate have been solved and refined to R-factors of 19.7, 19.1, and 17.8% at 2.0, 2.2, and 2.3 A resolution, respectively [3].

Associations of hisC with chemical compounds

  • The seventh step in the synthesis of histidine within eubacteria is carried out by a pyridoxal-5'-phosphate (PLP)-dependent l-histidinol phosphate aminotransferase (HisC, EC [4].
  • HspAT catalyzes the transfer of the amino group of L-histidinol phosphate (Hsp) to 2-oxoglutarate to form imidazole acetol phosphate (IAP) and glutamate [3].
  • 6. These data indicate that the strain of the Schiff base is the principal factor to decrease the pK(a) in HPAT and is crucial for the subsequent increase in the Schiff base pK(a) during catalysis, although the electrostatic effect of the arginine residue that binds the negatively charged group of the substrate is larger in HPAT than that in AspAT [5].
  • Histidinol phosphate aminotransferase (HPAT) is a pyridoxal 5'-phosphate (PLP)-dependent aminotransferase classified into Subgroup I aminotransferase, in which aspartate aminotransferase (AspAT) is the prototype [5].


  1. Cloning, structure, and expression of the Escherichia coli K-12 hisC gene. Grisolia, V., Carlomagno, M.S., Nappo, A.G., Bruni, C.B. J. Bacteriol. (1985) [Pubmed]
  2. The cysteine desulfurase IscS is required for synthesis of all five thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium. Nilsson, K., Lundgren, H.K., Hagervall, T.G., Björk, G.R. J. Bacteriol. (2002) [Pubmed]
  3. 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. Haruyama, K., Nakai, T., Miyahara, I., Hirotsu, K., Mizuguchi, H., Hayashi, H., Kagamiyama, H. Biochemistry (2001) [Pubmed]
  4. Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate. Sivaraman, J., Li, Y., Larocque, R., Schrag, J.D., Cygler, M., Matte, A. J. Mol. Biol. (2001) [Pubmed]
  5. Characterization of histidinol phosphate aminotransferase from Escherichia coli. Mizuguchi, H., Hayashi, H., Miyahara, I., Hirotsu, K., Kagamiyama, H. Biochim. Biophys. Acta (2003) [Pubmed]
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