MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:

Arabidopsis thaliana col: shikimate dehydrogenaseInferred from experiment: AT3G06350
Bacillus subtilis: shikimate 5-dehydrogenaseInferred from experiment: aroD
Escherichia coli K-12 substr. MG1655: shikimate dehydrogenaseInferred from experiment: aroE
shikimate dehydrogenase: ydiB
Methanocaldococcus jannaschii: shikimate dehydrogenaseInferred from experiment: aroE
Saccharomyces cerevisiae: pentafunctional AROM polypeptideInferred from experiment: ARO1

In Pathway: chorismate biosynthesis from 3-dehydroquinate

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Direct generic reaction:
shikimate + NAD(P)+ ← 3-dehydroshikimate + NAD(P)H + H+ (

Enzyme Commission Primary Name: shikimate dehydrogenase

Enzyme Commission Synonyms: dehydroshikimic reductase, shikimate oxidoreductase, shikimate:NADP+ oxidoreductase, 5-dehydroshikimate reductase, shikimate 5-dehydrogenase, 5-dehydroshikimic reductase, DHS reductase, shikimate:NADP+ 5-oxidoreductase, AroE

Standard Gibbs Free Energy (ΔrG in kcal/mol): -3.1764526Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
NAD+ cannot replace NADP+ [Yaniv55]. In higher organisms, this enzyme forms part of a multienzyme complex with EC, 3-dehydroquinate dehydratase [Chaudhuri85].

Citations: [BALINSKY61, MITSUHASHI54, Anton88, Ye03]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reaction of [L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+] (
i3: L-quinate + NAD+ → 3-dehydroquinate + NADH + H+ (

Instance reactions of [shikimate + NAD(P)+ ← 3-dehydroshikimate + NAD(P)H + H+] (
i1: shikimate + NADP+ ↔ 3-dehydroshikimate + NADPH + H+ (
i2: shikimate + NAD+ → 3-dehydroshikimate + NADH + H+ (1.1.1.-)

Unification Links: KEGG:R02413, Rhea:17737

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:O65917, UniProt:RELATED-TO:P07547, UniProt:RELATED-TO:P08566, UniProt:RELATED-TO:P0A6D5, UniProt:RELATED-TO:P15770, UniProt:RELATED-TO:Q9CES7, UniProt:RELATED-TO:Q9PIA0, UniProt:RELATED-TO:Q42947, UniProt:RELATED-TO:Q44606, UniProt:RELATED-TO:Q44608, UniProt:RELATED-TO:Q44609, UniProt:RELATED-TO:Q44610, UniProt:RELATED-TO:Q44611, UniProt:RELATED-TO:Q44612, UniProt:RELATED-TO:Q58484


Anton88: Anton IA, Coggins JR (1988). "Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase." Biochem J 1988;249(2);319-26. PMID: 3277621

BALINSKY61: BALINSKY D, DAVIES DD (1961). "Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase." Biochem J 80;292-6. PMID: 13686342

Chaudhuri85: Chaudhuri S, Coggins JR (1985). "The purification of shikimate dehydrogenase from Escherichia coli." Biochem J 1985;226(1);217-23. PMID: 3883995

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

MITSUHASHI54: MITSUHASHI S, DAVIS BD (1954). "Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase." Biochim Biophys Acta 15(2);268-80. PMID: 13208693

Yaniv55: YANIV H, GILVARG C (1955). "Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase." J Biol Chem 213(2);787-95. PMID: 14367339

Ye03: Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE (2003). "The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode." J Bacteriol 185(14);4144-51. PMID: 12837789

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.5 on Mon Nov 30, 2015, BIOCYC13A.