EC 1.1.1.282 - Quinate/shikimate dehydrogenase [NAD(P)+]

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IntEnz Enzyme Nomenclature
EC 1.1.1.282

Names

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

Reactions

Comments:

This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD+ or NADP+ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP+).

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]

[EC 1.1.1.282 created 2004]