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Literature summary extracted from

  • Peek, J.; Christendat, D.
    The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework (2015), Arch. Biochem. Biophys., 566, 85-99.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.25 drug development the essential enzyme is a potential target for antimicrobials Escherichia coli
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Staphylococcus aureus
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Mycobacterium tuberculosis
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Helicobacter pylori
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Aquifex aeolicus
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Pseudomonas putida
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Aspergillus nidulans
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Archaeoglobus fulgidus
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Corynebacterium glutamicum
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Staphylococcus epidermidis
1.1.1.25 drug development the essential enzyme is a potential target for herbicides and antimicrobials Toxoplasma gondii
1.1.1.282 drug development the essential enzyme is a potential target for herbicides and antimicrobials Corynebacterium glutamicum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.25 gene aroE, recombinant expression Corynebacterium glutamicum
1.1.1.282 gene cgR_0495, recombinant expression Corynebacterium glutamicum
1.1.1.282 gene qsuD, recombinant expression Corynebacterium glutamicum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.25 crystal structure analysis, PDB IDs 2GPT, 2O7Q, and 2O7S, for the binary and ternary complexes of enzyme and substrates Arabidopsis thaliana
1.1.1.25 crystal structure determination of apoenzyme, PDB ID 3DON, and shikimate-bound binary enzyme complex, PDB ID 3DOO Staphylococcus epidermidis
1.1.1.25 crystal structure determination of the apoenzyme, PDB ID 4OMU Pseudomonas putida
1.1.1.25 determination of diverse crystal structures with apoenzyme, or enzyme in binary or ternary complexes Helicobacter pylori
1.1.1.282 crystal structure analysis of binary and ternary complexes of enzyme and substrates, PDB IDs 3JYP, 2NLO, 3JYO, and 3JYQ Corynebacterium glutamicum
1.1.1.282 crystal structure determination as enzyme in binary complex with NAD+ (PDB ID 3JYO), or in ternary complex with shikimate and NADH (PDB ID 3JYQ), or in ternary complex with quinate and NADH (PDB ID 3JYP) Corynebacterium glutamicum

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.25 additional information the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Staphyococcus epidermidis SDH causes a substantial reduction in turnover rate Staphylococcus epidermidis
1.1.1.25 Q237A site-directed mutagenesis Helicobacter pylori
1.1.1.25 Q237K site-directed mutagenesis Helicobacter pylori
1.1.1.25 Q237N site-directed mutagenesis Helicobacter pylori
1.1.1.25 Y210A site-directed mutagenesis Helicobacter pylori
1.1.1.25 Y210S site-directed mutagenesis Helicobacter pylori

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.25 curcumin a noncompetitive inhibitor Helicobacter pylori
1.1.1.25 additional information inhibitor screening Helicobacter pylori

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.25 0.0091
-
 NADP+ pH 8.8, 25°C, with shikimate Toxoplasma gondii
1.1.1.25 0.0135
-
 NADP+ with shikimate, pH 7.0, 25°C Aspergillus nidulans
1.1.1.25 0.022
-
 NADP+ pH 7.0, 25°C, with shikimate Mycobacterium tuberculosis
1.1.1.25 0.03
-
 shikimate pH 9.0, 25°C, with NADP+ Mycobacterium tuberculosis
1.1.1.25 0.031
-
 NADPH pH 7.0, 25°C, with 3-dehydroshikimate Mycobacterium tuberculosis
1.1.1.25 0.031
-
 3-dehydroshikimate pH 7.0, 25°C, with NADPH Mycobacterium tuberculosis
1.1.1.25 0.0375
-
 shikimate pH not specified in the publication, 25°C, with NADP+ Staphylococcus aureus
1.1.1.25 0.0424
-
 NADP+ with shikimate, pH 9.0, 25°C Aquifex aeolicus
1.1.1.25 0.0425
-
 shikimate with NADP+, pH 9.0, 25°C Aquifex aeolicus
1.1.1.25 0.0426
-
 NADP+ pH not specified in the publication, 25°C, with shikimate Staphylococcus aureus
1.1.1.25 0.0502
-
 shikimate pH 7.0, 25°C, with NADP+ Mycobacterium tuberculosis
1.1.1.25 0.0527
-
 shikimate pH 8.8, 25°C, with NADP+ Toxoplasma gondii
1.1.1.25 0.055
-
 NADP+ pH 8.8, 25°C, with shikimate Pseudomonas putida
1.1.1.25 0.056
-
 NADP+ with shikimate, pH 9.0, 20°C Escherichia coli
1.1.1.25 0.063
-
 NADP+ pH 9.0, 25°C, with shikimate Mycobacterium tuberculosis
1.1.1.25 0.065
-
 shikimate with NADP+, pH 9.0, 20°C Escherichia coli
1.1.1.25 0.073
-
 shikimate pH 7.0, 25°C, with NADP+ Staphylococcus epidermidis
1.1.1.25 0.1
-
 NADP+ pH 7.0, 25°C, with shikimate Staphylococcus epidermidis
1.1.1.25 0.131
-
 NADP+ pH 8.8, 22°C, with shikimate Arabidopsis thaliana
1.1.1.25 0.14
-
 shikimate with NADP+, pH 9.0, 30°C Corynebacterium glutamicum
1.1.1.25 0.148
-
 shikimate with NADP+, pH 8.0, 25°C Helicobacter pylori
1.1.1.25 0.17
-
 shikimate with NADP+, pH 7.3, 87°C Archaeoglobus fulgidus
1.1.1.25 0.178
-
 shikimate pH 8.8, 25°C, with NADP+ Pseudomonas putida
1.1.1.25 0.182
-
 NADP+ with shikimate, pH 8.0, 25°C Helicobacter pylori
1.1.1.25 0.19
-
 NADP+ with shikimate, pH 7.3, 87°C Archaeoglobus fulgidus
1.1.1.25 0.223
-
 shikimate pH 8.5, 22°C, with NADP+, isozyme Poptr1 Populus trichocarpa
1.1.1.25 0.272
-
 3-dehydroshikimate with NADPH, pH 8.6, 30°C Corynebacterium glutamicum
1.1.1.25 0.311
-
 shikimate with NADP+, pH 7.0, 25°C Aspergillus nidulans
1.1.1.25 0.346
-
 shikimate pH 8.5, 22°C, with NADP+, isozyme Poptr5 Populus trichocarpa
1.1.1.25 0.685
-
 shikimate pH 8.8, 22°C, with NADP+ Arabidopsis thaliana
1.1.1.282 0.018
-
 NAD+ with shikimate, pH 8.6, 30°C Corynebacterium glutamicum
1.1.1.282 0.187
-
 shikimate with NADP+, pH 7.0, 30°C Corynebacterium glutamicum
1.1.1.282 0.2
-
 3-dehydroshikimate with NADPH, pH 7.0, 30°C Corynebacterium glutamicum
1.1.1.282 0.26
-
 shikimate with NAD+, pH 8.6, 30°C Corynebacterium glutamicum
1.1.1.282 2.541
-
 L-quinate with NADPH, pH 7.0, 30°C Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.25 3-dehydroshikimate + NADPH Populus trichocarpa
-
 shikimate + NADP+
-
 r
1.1.1.25 3-dehydroshikimate + NADPH Arabidopsis thaliana
-
 shikimate + NADP+
-
 r
1.1.1.25 shikimate + NADP+ Staphylococcus aureus
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Escherichia coli
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Mycobacterium tuberculosis
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Helicobacter pylori
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Aquifex aeolicus
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Pseudomonas putida
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Aspergillus nidulans
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Archaeoglobus fulgidus
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Corynebacterium glutamicum
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Staphylococcus epidermidis
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Toxoplasma gondii
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Archaeoglobus fulgidus ATCC 49558
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Aspergillus nidulans FGSC A4
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Staphylococcus epidermidis ATCC 35984
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+ Pseudomonas putida KT 2240
-
 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.282 L-quinate + NAD+ Corynebacterium glutamicum
-
 3-dehydroquinate + NADH + H+
-
 r
1.1.1.282 L-quinate + NAD+ Corynebacterium glutamicum ATCC 13032
-
 3-dehydroquinate + NADH + H+
-
 r
1.1.1.282 L-quinate + NADP+ Corynebacterium glutamicum
-
 3-dehydroquinate + NADPH + H+
-
 r
1.1.1.282 shikimate + NAD+ Corynebacterium glutamicum
-
 3-dehydroshikimate + NADH + H+
-
 r
1.1.1.282 shikimate + NAD+ Corynebacterium glutamicum ATCC 13032
-
 3-dehydroshikimate + NADH + H+
-
 r
1.1.1.282 shikimate + NADP+ Corynebacterium glutamicum
-
 3-dehydroshikimate + NADPH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.25 Aquifex aeolicus O67049
-
-
1.1.1.25 Arabidopsis thaliana Q9SQT8
-
-
1.1.1.25 Archaeoglobus fulgidus O27957
-
-
1.1.1.25 Archaeoglobus fulgidus ATCC 49558 O27957
-
-
1.1.1.25 Aspergillus nidulans P07547 shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
-
1.1.1.25 Aspergillus nidulans FGSC A4 P07547 shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
-
1.1.1.25 Corynebacterium glutamicum A4QB65
-
-
1.1.1.25 Escherichia coli
-
-
-
1.1.1.25 Helicobacter pylori
-
-
-
1.1.1.25 Mycobacterium tuberculosis
-
-
-
1.1.1.25 Populus trichocarpa
-
-
-
1.1.1.25 Pseudomonas putida Q88IJ7
-
-
1.1.1.25 Pseudomonas putida KT 2240 Q88IJ7
-
-
1.1.1.25 Staphylococcus aureus
-
-
-
1.1.1.25 Staphylococcus epidermidis Q5HNV1
-
-
1.1.1.25 Staphylococcus epidermidis ATCC 35984 Q5HNV1
-
-
1.1.1.25 Toxoplasma gondii Q6W3D0 shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
-
1.1.1.282 Corynebacterium glutamicum A4QB65
-
-
1.1.1.282 Corynebacterium glutamicum Q9X5C9
-
-
1.1.1.282 Corynebacterium glutamicum ATCC 13032 Q9X5C9
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.282 L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ catalytic reaction mechanism Corynebacterium glutamicum
a
1.1.1.282 shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+ catalytic reaction mechanism Corynebacterium glutamicum
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.25 732
-
 pH 7.3, 87°C Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.25 3-dehydroshikimate + NADPH
-
 Populus trichocarpa shikimate + NADP+
-
 r
1.1.1.25 3-dehydroshikimate + NADPH
-
 Arabidopsis thaliana shikimate + NADP+
-
 r
1.1.1.25 additional information no activity with quinate Helicobacter pylori ?
-
 ?
1.1.1.25 additional information no activity with quinate Pseudomonas putida ?
-
 ?
1.1.1.25 additional information no activity with quinate Archaeoglobus fulgidus ?
-
 ?
1.1.1.25 additional information no activity with quinate Staphylococcus epidermidis ?
-
 ?
1.1.1.25 additional information The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate Populus trichocarpa ?
-
 ?
1.1.1.25 additional information The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate Arabidopsis thaliana ?
-
 ?
1.1.1.25 additional information the SDH domain from the Toxoplasma gondii is part of the AROM complex. No activity with quinate Toxoplasma gondii ?
-
 ?
1.1.1.25 additional information no activity with quinate Archaeoglobus fulgidus ATCC 49558 ?
-
 ?
1.1.1.25 additional information no activity with quinate Staphylococcus epidermidis ATCC 35984 ?
-
 ?
1.1.1.25 additional information no activity with quinate Pseudomonas putida KT 2240 ?
-
 ?
1.1.1.25 shikimate + NADP+
-
 Staphylococcus aureus 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Escherichia coli 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Mycobacterium tuberculosis 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Helicobacter pylori 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Aquifex aeolicus 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Pseudomonas putida 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Aspergillus nidulans 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Archaeoglobus fulgidus 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Corynebacterium glutamicum 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Staphylococcus epidermidis 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Toxoplasma gondii 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Archaeoglobus fulgidus ATCC 49558 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Aspergillus nidulans FGSC A4 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Staphylococcus epidermidis ATCC 35984 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.25 shikimate + NADP+
-
 Pseudomonas putida KT 2240 3-dehydroshikimate + NADPH + H+
-
 r
1.1.1.282 L-quinate + NAD+
-
 Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
 r
1.1.1.282 L-quinate + NAD+
-
 Corynebacterium glutamicum ATCC 13032 3-dehydroquinate + NADH + H+
-
 r
1.1.1.282 L-quinate + NADP+
-
 Corynebacterium glutamicum 3-dehydroquinate + NADPH + H+
-
 r
1.1.1.282 additional information the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity Corynebacterium glutamicum ?
-
 ?
1.1.1.282 additional information the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity Corynebacterium glutamicum ATCC 13032 ?
-
 ?
1.1.1.282 shikimate + NAD+
-
 Corynebacterium glutamicum 3-dehydroshikimate + NADH + H+
-
 r
1.1.1.282 shikimate + NAD+
-
 Corynebacterium glutamicum ATCC 13032 3-dehydroshikimate + NADH + H+
-
 r
1.1.1.282 shikimate + NADP+
-
 Corynebacterium glutamicum 3-dehydroshikimate + NADPH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.25 dimer
-
 Mycobacterium tuberculosis
1.1.1.25 dimer
-
 Corynebacterium glutamicum
1.1.1.25 monomer
-
 Escherichia coli
1.1.1.25 monomer
-
 Staphylococcus epidermidis
1.1.1.25 monomer in solution Arabidopsis thaliana
1.1.1.25 More SDH enzymes exist in opened and closed conformational states. In the ternary structure of Aquifex aeolicus SDH (PDB ID 2HK9), three loops in the shikimate binding domain are shifted about 5 A toward the NADP++ binding site compared to their position in an unliganded structure of the same enzyme (PDB ID 2HK8). The closed form of the structure thus brings the bound shikimate and NADP+ molecules into close proximity, facilitating a hydride transfer between the shikimate C5-hydroxyl and C4 of the NADP+ nicotinamide ring Aquifex aeolicus
1.1.1.25 More the SDH domain is connected via its N-terminus to the DHQ module Arabidopsis thaliana
1.1.1.282 dimer
-
 Corynebacterium glutamicum

Synonyms

EC Number Synonyms Comment Organism
1.1.1.25 AroE
-
 Aquifex aeolicus
1.1.1.25 AroE
-
 Archaeoglobus fulgidus
1.1.1.25 dehydroquinate dehydratase/shikimate dehydrogenase
-
 Populus trichocarpa
1.1.1.25 dehydroquinate dehydratase/shikimate dehydrogenase
-
 Arabidopsis thaliana
1.1.1.25 DQD/SDH
-
 Populus trichocarpa
1.1.1.25 DQD/SDH
-
 Arabidopsis thaliana
1.1.1.25 SDH
-
 Staphylococcus aureus
1.1.1.25 SDH
-
 Escherichia coli
1.1.1.25 SDH
-
 Mycobacterium tuberculosis
1.1.1.25 SDH
-
 Helicobacter pylori
1.1.1.25 SDH
-
 Aquifex aeolicus
1.1.1.25 SDH
-
 Pseudomonas putida
1.1.1.25 SDH
-
 Aspergillus nidulans
1.1.1.25 SDH
-
 Archaeoglobus fulgidus
1.1.1.25 SDH
-
 Corynebacterium glutamicum
1.1.1.25 SDH
-
 Staphylococcus epidermidis
1.1.1.25 SDH
-
 Toxoplasma gondii
1.1.1.25 YdiB
-
 Escherichia coli
1.1.1.282 quinate/shikimate dehydrogenase
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.25 20
-
 assay at Escherichia coli
1.1.1.25 22
-
 assay at room temperature Populus trichocarpa
1.1.1.25 22
-
 shikimate oxidation assay at room temperature Arabidopsis thaliana
1.1.1.25 25
-
 assay at Staphylococcus aureus
1.1.1.25 25
-
 assay at Mycobacterium tuberculosis
1.1.1.25 25
-
 assay at Aquifex aeolicus
1.1.1.25 25
-
 assay at Pseudomonas putida
1.1.1.25 25
-
 assay at Aspergillus nidulans
1.1.1.25 25
-
 assay at Staphylococcus epidermidis
1.1.1.25 25
-
 assay at Toxoplasma gondii
1.1.1.25 30
-
 assay at Corynebacterium glutamicum
1.1.1.25 87
-
 assay at Archaeoglobus fulgidus
1.1.1.282 30
-
 assay at Corynebacterium glutamicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.25 1.5
-
 shikimate with NADP+, pH 7.0, 25°C Aspergillus nidulans
1.1.1.25 2.77
-
 NADP+ pH 8.8, 25°C, with shikimate Toxoplasma gondii
1.1.1.25 2.78
-
 shikimate pH 8.8, 25°C, with NADP+ Toxoplasma gondii
1.1.1.25 5.9
-
 NADP+ pH 7.0, 25°C, with shikimate Mycobacterium tuberculosis
1.1.1.25 7.1
-
 NADP+ with shikimate, pH 8.0, 25°C Helicobacter pylori
1.1.1.25 7.7
-
 shikimate with NADP+, pH 8.0, 25°C Helicobacter pylori
1.1.1.25 8.2
-
 shikimate pH 7.0, 25°C, with NADP+ Mycobacterium tuberculosis
1.1.1.25 22.8
-
 shikimate pH 7.0, 25°C, with NADP+ Staphylococcus epidermidis
1.1.1.25 22.8
-
 NADP+ pH 7.0, 25°C, with shikimate Staphylococcus epidermidis
1.1.1.25 45
-
 NADPH pH 7.0, 25°C, with 3-dehydroshikimate Mycobacterium tuberculosis
1.1.1.25 49
-
 3-dehydroshikimate pH 7.0, 25°C, with NADPH Mycobacterium tuberculosis
1.1.1.25 55.5
-
 shikimate with NADP+, pH 9.0, 25°C Aquifex aeolicus
1.1.1.25 55.5
-
 NADP+ with shikimate, pH 9.0, 25°C Aquifex aeolicus
1.1.1.25 118
-
 3-dehydroshikimate with NADPH, pH 8.6, 30°C Corynebacterium glutamicum
1.1.1.25 135.8
-
 shikimate pH not specified in the publication, 25°C, with NADP+ Staphylococcus aureus
1.1.1.25 146.2
-
 NADP+ pH not specified in the publication, 25°C, with shikimate Staphylococcus aureus
1.1.1.25 234
-
 shikimate with NADP+, pH 9.0, 30°C Corynebacterium glutamicum
1.1.1.25 237
-
 shikimate with NADP+, pH 9.0, 20°C Escherichia coli
1.1.1.25 237
-
 NADP+ with shikimate, pH 9.0, 20°C Escherichia coli
1.1.1.25 302
-
 NADP+ pH 8.8, 25°C, with shikimate Pseudomonas putida
1.1.1.25 307
-
 shikimate pH 8.8, 25°C, with NADP+ Pseudomonas putida
1.1.1.25 390
-
 NADP+ with shikimate, pH 7.3, 87°C Archaeoglobus fulgidus
1.1.1.25 399
-
 NADP+ pH 8.8, 22°C, with shikimate Arabidopsis thaliana
1.1.1.25 399
-
 shikimate pH 9.0, 25°C, with NADP+ Mycobacterium tuberculosis
1.1.1.25 399
-
 NADP+ pH 9.0, 25°C, with shikimate Mycobacterium tuberculosis
1.1.1.25 428
-
 shikimate pH 8.8, 22°C, with NADP+ Arabidopsis thaliana
1.1.1.282 0.036
-
 L-quinate with NADPH, pH 7.0, 30°C Corynebacterium glutamicum
1.1.1.282 9.6
-
 shikimate with NAD+, pH 8.6, 30°C Corynebacterium glutamicum
1.1.1.282 31.1
-
 shikimate with NADP+, pH 7.0, 30°C Corynebacterium glutamicum
1.1.1.282 329
-
 3-dehydroshikimate with NADPH, pH 7.0, 30°C Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.25 7
-
 assay at Aspergillus nidulans
1.1.1.25 7 9 assay at Mycobacterium tuberculosis
1.1.1.25 7.3
-
 assay at Archaeoglobus fulgidus
1.1.1.25 8
-
 assay at Staphylococcus epidermidis
1.1.1.25 8.5
-
 assay at Populus trichocarpa
1.1.1.25 8.8
-
 assay at Pseudomonas putida
1.1.1.25 8.8
-
 assay at Toxoplasma gondii
1.1.1.25 8.8
-
 shikimate oxidation assay at Arabidopsis thaliana
1.1.1.25 9
-
 assay at Escherichia coli
1.1.1.25 9
-
 assay at Aquifex aeolicus
1.1.1.25 9
-
 assay at Corynebacterium glutamicum
1.1.1.282 7
-
 assay at Corynebacterium glutamicum
1.1.1.282 8.6
-
 assay at Corynebacterium glutamicum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.25 7 9 at pH 7.0, the forward reaction catalyzed by Corynebacterium glutamicum SDH proceeds at a rate about 10fold faster than the reverse reaction Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.25 additional information cofactor binding might trigger domain movement Staphylococcus epidermidis
1.1.1.25 NADP+ dependent on Staphylococcus aureus
1.1.1.25 NADP+ dependent on Escherichia coli
1.1.1.25 NADP+ dependent on Mycobacterium tuberculosis
1.1.1.25 NADP+ dependent on Helicobacter pylori
1.1.1.25 NADP+ dependent on Aquifex aeolicus
1.1.1.25 NADP+ dependent on Pseudomonas putida
1.1.1.25 NADP+ dependent on Aspergillus nidulans
1.1.1.25 NADP+ dependent on Archaeoglobus fulgidus
1.1.1.25 NADP+ dependent on Corynebacterium glutamicum
1.1.1.25 NADP+ dependent on Staphylococcus epidermidis
1.1.1.25 NADP+ dependent on Toxoplasma gondii
1.1.1.25 NADPH dependent on Staphylococcus aureus
1.1.1.25 NADPH dependent on Escherichia coli
1.1.1.25 NADPH dependent on Mycobacterium tuberculosis
1.1.1.25 NADPH dependent on Helicobacter pylori
1.1.1.25 NADPH dependent on Aquifex aeolicus
1.1.1.25 NADPH dependent on Pseudomonas putida
1.1.1.25 NADPH dependent on Aspergillus nidulans
1.1.1.25 NADPH dependent on Archaeoglobus fulgidus
1.1.1.25 NADPH dependent on Corynebacterium glutamicum
1.1.1.25 NADPH dependent on Staphylococcus epidermidis
1.1.1.25 NADPH dependent on Toxoplasma gondii
1.1.1.282 NAD+ dependent on Corynebacterium glutamicum
1.1.1.282 NADH dependent on Corynebacterium glutamicum
1.1.1.282 NADP+
-
 Corynebacterium glutamicum
1.1.1.282 NADPH
-
 Corynebacterium glutamicum

General Information

EC Number General Information Comment Organism
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Staphylococcus aureus
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Escherichia coli
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Mycobacterium tuberculosis
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Helicobacter pylori
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Aquifex aeolicus
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Pseudomonas putida
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Aspergillus nidulans
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Archaeoglobus fulgidus
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Corynebacterium glutamicum
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Staphylococcus epidermidis
1.1.1.25 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Toxoplasma gondii
1.1.1.25 malfunction a contact with the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Arabidopsis thaliana DHQ-SDH causes a substantial reduction in turnover rate Arabidopsis thaliana
1.1.1.25 metabolism in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway, (B) the quinate pathway, (C) the aminoshikimate pathway, overview Arabidopsis thaliana
1.1.1.25 metabolism in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway. (B) the quinate pathway. (C) the aminoshikimate pathway, overview Populus trichocarpa
1.1.1.25 metabolism the enzyme catalyze the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Toxoplasma gondii
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Staphylococcus aureus
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Escherichia coli
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Mycobacterium tuberculosis
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Helicobacter pylori
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Aquifex aeolicus
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Pseudomonas putida
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Archaeoglobus fulgidus
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Corynebacterium glutamicum
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Staphylococcus epidermidis
1.1.1.25 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites. SDH is part of the Arom complex, that catalyzes both the third and fourth reactions in the shikimate pathway. This large enzyme complex contains five functional domains that are equivalent to the monofunctional enzymes (in bacteria) catalyzing reactions two through six of the shikimate pathway Aspergillus nidulans
1.1.1.25 additional information in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQ-SDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQ-SDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processe. Crystallization of the Arabidopsis thaliana protein with shikimate bound in the SDH domain and tartrate (a component of the crystallization solution) in the DHQ domain reveals a V-shaped orientation of the domains. Addition of NADP+ to DHQ–SDH crystals already containing shikimate in the SDH domain results in the production of 3-dehydroshikimate by the SDH domain and the transfer of the compound to the DHQ active sites Arabidopsis thaliana
1.1.1.25 additional information in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQ–SDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQ–SDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processes Populus trichocarpa
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Staphylococcus aureus
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Escherichia coli
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Mycobacterium tuberculosis
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Helicobacter pylori
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Pseudomonas putida
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Aspergillus nidulans
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Archaeoglobus fulgidus
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Corynebacterium glutamicum
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Staphylococcus epidermidis
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes Toxoplasma gondii
1.1.1.25 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes, the enzyme reaction represents the fourth step of the shikimate pathway Aquifex aeolicus
1.1.1.282 evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Corynebacterium glutamicum
1.1.1.282 malfunction disruption of the qdh gene in prevents growth on both compounds, demonstrating the important role of the enzyme in hydroaromatic catabolism Corynebacterium glutamicum
1.1.1.282 metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Corynebacterium glutamicum
1.1.1.282 physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes. The reduced efficiency of Corynebacterium glutamicum enzyme with shikimate as a substrate may also result in part from the flexibility of the catalytic group, Lys73, which adopts multiple conformations in the shikimate-liganded enzyme structure Corynebacterium glutamicum