Category:Complex:HISTDEHYD-CPLX

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Comments (originally from EcoCyc[1][2]) The catalytically active form of this bifunctional enzyme has been shown to be a dimer.[3][4][3][5]

intragenic complementation occurs


References

  1. ↑ EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  2. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 Chiariotti, L et al. (1986) Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region. Mol. Gen. Genet. 203 382-8 PubMed
  4. ↑ Bürger, E & Görisch, H (1981) Evidence for an essential lysine at the active site of L-histidinol:NAD+ oxidoreductase; a bifunctional dehydrogenase. Eur. J. Biochem. 118 125-30 PubMed
  5. ↑ Bruni, CB et al. (1986) Primary and secondary structural homologies between the HIS4 gene product of Saccharomyces cerevisiae and the hisIE and hisD gene products of Escherichia coli and Salmonella typhimurium. Mol. Gen. Genet. 203 389-96 PubMed

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