EC 1.1.1.282 - Quinate/shikimate dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.1.1.282

Names

Accepted name:
quinate/shikimate dehydrogenase
Other names:
YdiB
quinate dehydrogenase
quinic dehydrogenase
Systematic name:
L-quinate:NAD(P)+ 3-oxidoreductase

Reactions

Comments:

The enzyme is found in bacteria (mostly, but not exclusively, Gram-positive bacteria), fungi, and plants. It participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0030266 , GO:0052733 , GO:0052734 , GO:0004764
UniProtKB/Swiss-Prot: (37) [show] [UniProt]

References

  1. Michel, G., Roszak, A.W., Sauvé, V., Maclean, J., Matte, A., Coggins, J.R., Cygler, M. and Lapthorn, A.J.
    Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activities.
    J. Biol. Chem. 278 : 19463-19472 (2003). [PMID: 12637497]
  2. Benach, J., Lee, I., Edstrom, W., Kuzin, A.P., Chiang, Y., Acton, T.B., Montelione, G.T., Hunt and J.F.
    The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.
    J. Biol. Chem. 278 : 19176-19182 (2003). [PMID: 12624088]
  3. Mitsuhashi, S., Davis, B. D.
    Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase.
    Biochim. Biophys. Acta 15 : 268-280 (1954). [PMID: 13208693]
  4. Gamborg, O.L.
    Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures.
    Biochim. Biophys. Acta 128 : 483-491 (1966).
  5. Hawkins, A. R., Giles, N. H., Kinghorn, J. R.
    Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans.
    Biochem. Genet. 20 : 271-286 (1982). [PMID: 7049157]
  6. Singh, S., Stavrinides, J., Christendat, D., Guttman, D. S.
    A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass.
    Mol. Biol. Evol. 25 : 2221-2232 (2008). [PMID: 18669580]
  7. Teramoto, H., Inui, M., Yukawa, H.
    Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum.
    Appl. Environ. Microbiol. 75 : 3461-3468 (2009). [PMID: 19376919]
  8. Kubota, T., Tanaka, Y., Hiraga, K., Inui, M., Yukawa, H.
    Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum.
    Appl. Microbiol. Biotechnol. 97 : 8139-8149 (2013). [PMID: 23306642]
  9. Peek, J., Christendat, D.
    The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework.
    Arch. Biochem. Biophys. 566 : 85-99 (2015). [PMID: 25524738]

[EC 1.1.1.282 created 2004]