The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

hisD  -  bifunctional histidinal dehydrogenase/...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2015, JW2002
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of hisD


High impact information on hisD


Chemical compound and disease context of hisD


Biological context of hisD

  • A comparative analysis of the different transcriptional and translational control elements within the two operons reveals a remarkable preservation for most of them except for the intercistronic region between the first (hisG) and second (hisD) structural genes and for the rho-independent terminator of transcription at the end of the operon [12].
  • Another plasmid (pCB5) contained the hisG gene and part of the hisD gene [13].
  • Two other contiguous open reading frames oriented divergently with respect to hisD did not show significant similarity with any of the his genes or to other sequences included in the gene bank [3].

Associations of hisD with chemical compounds


Other interactions of hisD


Analytical, diagnostic and therapeutic context of hisD

  • The relative positions of these peptides were deduced by aligning their sequences with the sequence of the HIS4C gene product of Saccharomyces cerevisiae. cDNA encoding histidinol dehydrogenase was then amplified from a library using a polymerase chain reaction primed with degenerate oligonucleotide pools of known position and orientation [14].


  1. Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region. Chiariotti, L., Alifano, P., Carlomagno, M.S., Bruni, C.B. Mol. Gen. Genet. (1986) [Pubmed]
  2. Isolation and characterization of the hisG and hisD genes of Klebsiella pneumoniae. Rodriguez, R.L., West, R.W., Tait, R.C., Jaynes, J.M., Shanmugam, K.T. Gene (1981) [Pubmed]
  3. Further characterization of the histidine gene cluster of Streptomyces coelicolor A3(2): nucleotide sequence and transcriptional analysis of hisD. Limauro, D., Avitabile, A., Puglia, A.M., Bruni, C.B. Res. Microbiol. (1992) [Pubmed]
  4. Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. Barbosa, J.A., Sivaraman, J., Li, Y., Larocque, R., Matte, A., Schrag, J.D., Cygler, M. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  5. Two dominant-acting selectable markers for gene transfer studies in mammalian cells. Hartman, S.C., Mulligan, R.C. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  6. Cloning of mycobacterial histidine synthesis genes by complementation of a Mycobacterium smegmatis auxotroph. Hinshelwood, S., Stoker, N.G. Mol. Microbiol. (1992) [Pubmed]
  7. New vectors in fission yeast: application for cloning the his2 gene. Weilguny, D., Praetorius, M., Carr, A., Egel, R., Nielsen, O. Gene (1991) [Pubmed]
  8. Nucleotide and amino acid polymorphism in the gene for L-histidinol dehydrogenase of Escherichia coli K12. Jovanović, G., Kostić, T., Savić, D.J. Nucleic Acids Res. (1990) [Pubmed]
  9. Absence of insertions among spontaneous mutants of Salmonella typhimurium. Casadesus, J., Roth, J.R. Mol. Gen. Genet. (1989) [Pubmed]
  10. Evidence for an essential lysine at the active site of L-histidinol:NAD+ oxidoreductase; a bifunctional dehydrogenase. Bürger, E., Görisch, H. Eur. J. Biochem. (1981) [Pubmed]
  11. Immunoadsorption of histidinol dehydrogenase in the presence of urea. Andorn, N., Aronovitch, J. J. Immunol. Methods (1984) [Pubmed]
  12. Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons. Carlomagno, M.S., Chiariotti, L., Alifano, P., Nappo, A.G., Bruni, C.B. J. Mol. Biol. (1988) [Pubmed]
  13. Structural and physiological studies of the Escherichia coli histidine operon inserted into plasmid vectors. Bruni, C.B., Musti, A.M., Frunzio, R., Blasi, F. J. Bacteriol. (1980) [Pubmed]
  14. Structural and functional conservation of histidinol dehydrogenase between plants and microbes. Nagai, A., Ward, E., Beck, J., Tada, S., Chang, J.Y., Scheidegger, A., Ryals, J. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
WikiGenes - Universities