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Literature summary for 1.1.1.25 extracted from
- The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework (2015), Arch. Biochem. Biophys., 566, 85-99.
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the essential enzyme is a potential target for antimicrobials | Escherichia coli |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Staphylococcus aureus |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Mycobacterium tuberculosis |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Helicobacter pylori |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Aquifex aeolicus |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Pseudomonas putida |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Aspergillus nidulans |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Archaeoglobus fulgidus |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Corynebacterium glutamicum |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Staphylococcus epidermidis |
| drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Toxoplasma gondii |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene aroE, recombinant expression | Corynebacterium glutamicum |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis, PDB IDs 2GPT, 2O7Q, and 2O7S, for the binary and ternary complexes of enzyme and substrates | Arabidopsis thaliana |
| crystal structure determination of apoenzyme, PDB ID 3DON, and shikimate-bound binary enzyme complex, PDB ID 3DOO | Staphylococcus epidermidis |
| crystal structure determination of the apoenzyme, PDB ID 4OMU | Pseudomonas putida |
| determination of diverse crystal structures with apoenzyme, or enzyme in binary or ternary complexes | Helicobacter pylori |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 |
| Q237A | site-directed mutagenesis | Helicobacter pylori |
| Q237K | site-directed mutagenesis | Helicobacter pylori |
| Q237N | site-directed mutagenesis | Helicobacter pylori |
| Y210A | site-directed mutagenesis | Helicobacter pylori |
| Y210S | site-directed mutagenesis | Helicobacter pylori |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| curcumin | a noncompetitive inhibitor | Helicobacter pylori |  |
| additional information | inhibitor screening | Helicobacter pylori |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0091 | - |
NADP+ | pH 8.8, 25°C, with shikimate | Toxoplasma gondii | |
| 0.0135 | - |
NADP+ | with shikimate, pH 7.0, 25°C | Aspergillus nidulans | |
| 0.022 | - |
NADP+ | pH 7.0, 25°C, with shikimate | Mycobacterium tuberculosis | |
| 0.03 | - |
shikimate | pH 9.0, 25°C, with NADP+ | Mycobacterium tuberculosis | |
| 0.031 | - |
NADPH | pH 7.0, 25°C, with 3-dehydroshikimate | Mycobacterium tuberculosis | |
| 0.031 | - |
3-dehydroshikimate | pH 7.0, 25°C, with NADPH | Mycobacterium tuberculosis | |
| 0.0375 | - |
shikimate | pH not specified in the publication, 25°C, with NADP+ | Staphylococcus aureus | |
| 0.0424 | - |
NADP+ | with shikimate, pH 9.0, 25°C | Aquifex aeolicus | |
| 0.0425 | - |
shikimate | with NADP+, pH 9.0, 25°C | Aquifex aeolicus | |
| 0.0426 | - |
NADP+ | pH not specified in the publication, 25°C, with shikimate | Staphylococcus aureus | |
| 0.0502 | - |
shikimate | pH 7.0, 25°C, with NADP+ | Mycobacterium tuberculosis | |
| 0.0527 | - |
shikimate | pH 8.8, 25°C, with NADP+ | Toxoplasma gondii | |
| 0.055 | - |
NADP+ | pH 8.8, 25°C, with shikimate | Pseudomonas putida | |
| 0.056 | - |
NADP+ | with shikimate, pH 9.0, 20°C | Escherichia coli | |
| 0.063 | - |
NADP+ | pH 9.0, 25°C, with shikimate | Mycobacterium tuberculosis | |
| 0.065 | - |
shikimate | with NADP+, pH 9.0, 20°C | Escherichia coli | |
| 0.073 | - |
shikimate | pH 7.0, 25°C, with NADP+ | Staphylococcus epidermidis | |
| 0.1 | - |
NADP+ | pH 7.0, 25°C, with shikimate | Staphylococcus epidermidis | |
| 0.131 | - |
NADP+ | pH 8.8, 22°C, with shikimate | Arabidopsis thaliana | |
| 0.14 | - |
shikimate | with NADP+, pH 9.0, 30°C | Corynebacterium glutamicum | |
| 0.148 | - |
shikimate | with NADP+, pH 8.0, 25°C | Helicobacter pylori | |
| 0.17 | - |
shikimate | with NADP+, pH 7.3, 87°C | Archaeoglobus fulgidus | |
| 0.178 | - |
shikimate | pH 8.8, 25°C, with NADP+ | Pseudomonas putida | |
| 0.182 | - |
NADP+ | with shikimate, pH 8.0, 25°C | Helicobacter pylori | |
| 0.19 | - |
NADP+ | with shikimate, pH 7.3, 87°C | Archaeoglobus fulgidus | |
| 0.223 | - |
shikimate | pH 8.5, 22°C, with NADP+, isozyme Poptr1 | Populus trichocarpa | |
| 0.272 | - |
3-dehydroshikimate | with NADPH, pH 8.6, 30°C | Corynebacterium glutamicum | |
| 0.311 | - |
shikimate | with NADP+, pH 7.0, 25°C | Aspergillus nidulans | |
| 0.346 | - |
shikimate | pH 8.5, 22°C, with NADP+, isozyme Poptr5 | Populus trichocarpa | |
| 0.685 | - |
shikimate | pH 8.8, 22°C, with NADP+ | Arabidopsis thaliana | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-dehydroshikimate + NADPH | Populus trichocarpa | - |
shikimate + NADP+ | - |
r | |
| 3-dehydroshikimate + NADPH | Arabidopsis thaliana | - |
shikimate + NADP+ | - |
r | |
| shikimate + NADP+ | Staphylococcus aureus | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Escherichia coli | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Mycobacterium tuberculosis | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Helicobacter pylori | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Aquifex aeolicus | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Pseudomonas putida | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Aspergillus nidulans | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Archaeoglobus fulgidus | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Corynebacterium glutamicum | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Staphylococcus epidermidis | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Toxoplasma gondii | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Archaeoglobus fulgidus ATCC 49558 | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Aspergillus nidulans FGSC A4 | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Staphylococcus epidermidis ATCC 35984 | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | Pseudomonas putida KT 2240 | - |
3-dehydroshikimate + NADPH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aquifex aeolicus | O67049 | - |
- |
| Arabidopsis thaliana | Q9SQT8 | - |
- |
| Archaeoglobus fulgidus | O27957 | - |
- |
| Archaeoglobus fulgidus ATCC 49558 | O27957 | - |
- |
| Aspergillus nidulans | P07547 | shikimate dehydrogenase as part of the pentafunctional AROM polypeptide | - |
| Aspergillus nidulans FGSC A4 | P07547 | shikimate dehydrogenase as part of the pentafunctional AROM polypeptide | - |
| Corynebacterium glutamicum | A4QB65 | - |
- |
| Escherichia coli | - |
- |
- |
| Helicobacter pylori | - |
- |
- |
| Mycobacterium tuberculosis | - |
- |
- |
| Populus trichocarpa | - |
- |
- |
| Pseudomonas putida | Q88IJ7 | - |
- |
| Pseudomonas putida KT 2240 | Q88IJ7 | - |
- |
| Staphylococcus aureus | - |
- |
- |
| Staphylococcus epidermidis | Q5HNV1 | - |
- |
| Staphylococcus epidermidis ATCC 35984 | Q5HNV1 | - |
- |
| Toxoplasma gondii | Q6W3D0 | shikimate dehydrogenase as part of the pentafunctional AROM polypeptide | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 732 | - |
pH 7.3, 87°C | Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-dehydroshikimate + NADPH | - |
Populus trichocarpa | shikimate + NADP+ | - |
r | |
| 3-dehydroshikimate + NADPH | - |
Arabidopsis thaliana | shikimate + NADP+ | - |
r | |
| additional information | no activity with quinate | Helicobacter pylori | ? | - |
? | |
| additional information | no activity with quinate | Pseudomonas putida | ? | - |
? | |
| additional information | no activity with quinate | Archaeoglobus fulgidus | ? | - |
? | |
| additional information | no activity with quinate | Staphylococcus epidermidis | ? | - |
? | |
| additional information | The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate | Populus trichocarpa | ? | - |
? | |
| additional information | The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate | Arabidopsis thaliana | ? | - |
? | |
| additional information | the SDH domain from the Toxoplasma gondii is part of the AROM complex. No activity with quinate | Toxoplasma gondii | ? | - |
? | |
| additional information | no activity with quinate | Archaeoglobus fulgidus ATCC 49558 | ? | - |
? | |
| additional information | no activity with quinate | Staphylococcus epidermidis ATCC 35984 | ? | - |
? | |
| additional information | no activity with quinate | Pseudomonas putida KT 2240 | ? | - |
? | |
| shikimate + NADP+ | - |
Staphylococcus aureus | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Escherichia coli | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Mycobacterium tuberculosis | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Helicobacter pylori | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Aquifex aeolicus | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Pseudomonas putida | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Aspergillus nidulans | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Archaeoglobus fulgidus | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Corynebacterium glutamicum | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Staphylococcus epidermidis | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Toxoplasma gondii | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Archaeoglobus fulgidus ATCC 49558 | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Aspergillus nidulans FGSC A4 | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Staphylococcus epidermidis ATCC 35984 | 3-dehydroshikimate + NADPH + H+ | - |
r | |
| shikimate + NADP+ | - |
Pseudomonas putida KT 2240 | 3-dehydroshikimate + NADPH + H+ | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Mycobacterium tuberculosis |
| dimer | - |
Corynebacterium glutamicum |
| monomer | - |
Escherichia coli |
| monomer | - |
Staphylococcus epidermidis |
| monomer | in solution | Arabidopsis thaliana |
| 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 |
| More | the SDH domain is connected via its N-terminus to the DHQ module | Arabidopsis thaliana |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AroE | - |
Aquifex aeolicus |
| AroE | - |
Archaeoglobus fulgidus |
| dehydroquinate dehydratase/shikimate dehydrogenase | - |
Populus trichocarpa |
| dehydroquinate dehydratase/shikimate dehydrogenase | - |
Arabidopsis thaliana |
| DQD/SDH | - |
Populus trichocarpa |
| DQD/SDH | - |
Arabidopsis thaliana |
| SDH | - |
Staphylococcus aureus |
| SDH | - |
Escherichia coli |
| SDH | - |
Mycobacterium tuberculosis |
| SDH | - |
Helicobacter pylori |
| SDH | - |
Aquifex aeolicus |
| SDH | - |
Pseudomonas putida |
| SDH | - |
Aspergillus nidulans |
| SDH | - |
Archaeoglobus fulgidus |
| SDH | - |
Corynebacterium glutamicum |
| SDH | - |
Staphylococcus epidermidis |
| SDH | - |
Toxoplasma gondii |
| YdiB | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
assay at | Escherichia coli |
| 22 | - |
assay at room temperature | Populus trichocarpa |
| 22 | - |
shikimate oxidation assay at room temperature | Arabidopsis thaliana |
| 25 | - |
assay at | Staphylococcus aureus |
| 25 | - |
assay at | Mycobacterium tuberculosis |
| 25 | - |
assay at | Aquifex aeolicus |
| 25 | - |
assay at | Pseudomonas putida |
| 25 | - |
assay at | Aspergillus nidulans |
| 25 | - |
assay at | Staphylococcus epidermidis |
| 25 | - |
assay at | Toxoplasma gondii |
| 30 | - |
assay at | Corynebacterium glutamicum |
| 87 | - |
assay at | Archaeoglobus fulgidus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.5 | - |
shikimate | with NADP+, pH 7.0, 25°C | Aspergillus nidulans | |
| 2.77 | - |
NADP+ | pH 8.8, 25°C, with shikimate | Toxoplasma gondii | |
| 2.78 | - |
shikimate | pH 8.8, 25°C, with NADP+ | Toxoplasma gondii | |
| 5.9 | - |
NADP+ | pH 7.0, 25°C, with shikimate | Mycobacterium tuberculosis | |
| 7.1 | - |
NADP+ | with shikimate, pH 8.0, 25°C | Helicobacter pylori | |
| 7.7 | - |
shikimate | with NADP+, pH 8.0, 25°C | Helicobacter pylori | |
| 8.2 | - |
shikimate | pH 7.0, 25°C, with NADP+ | Mycobacterium tuberculosis | |
| 22.8 | - |
shikimate | pH 7.0, 25°C, with NADP+ | Staphylococcus epidermidis | |
| 22.8 | - |
NADP+ | pH 7.0, 25°C, with shikimate | Staphylococcus epidermidis | |
| 45 | - |
NADPH | pH 7.0, 25°C, with 3-dehydroshikimate | Mycobacterium tuberculosis | |
| 49 | - |
3-dehydroshikimate | pH 7.0, 25°C, with NADPH | Mycobacterium tuberculosis | |
| 55.5 | - |
shikimate | with NADP+, pH 9.0, 25°C | Aquifex aeolicus | |
| 55.5 | - |
NADP+ | with shikimate, pH 9.0, 25°C | Aquifex aeolicus | |
| 118 | - |
3-dehydroshikimate | with NADPH, pH 8.6, 30°C | Corynebacterium glutamicum | |
| 135.8 | - |
shikimate | pH not specified in the publication, 25°C, with NADP+ | Staphylococcus aureus | |
| 146.2 | - |
NADP+ | pH not specified in the publication, 25°C, with shikimate | Staphylococcus aureus | |
| 234 | - |
shikimate | with NADP+, pH 9.0, 30°C | Corynebacterium glutamicum | |
| 237 | - |
shikimate | with NADP+, pH 9.0, 20°C | Escherichia coli | |
| 237 | - |
NADP+ | with shikimate, pH 9.0, 20°C | Escherichia coli | |
| 302 | - |
NADP+ | pH 8.8, 25°C, with shikimate | Pseudomonas putida | |
| 307 | - |
shikimate | pH 8.8, 25°C, with NADP+ | Pseudomonas putida | |
| 390 | - |
NADP+ | with shikimate, pH 7.3, 87°C | Archaeoglobus fulgidus | |
| 399 | - |
NADP+ | pH 8.8, 22°C, with shikimate | Arabidopsis thaliana | |
| 399 | - |
shikimate | pH 9.0, 25°C, with NADP+ | Mycobacterium tuberculosis | |
| 399 | - |
NADP+ | pH 9.0, 25°C, with shikimate | Mycobacterium tuberculosis | |
| 428 | - |
shikimate | pH 8.8, 22°C, with NADP+ | Arabidopsis thaliana | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Aspergillus nidulans |
| 7 | 9 | assay at | Mycobacterium tuberculosis |
| 7.3 | - |
assay at | Archaeoglobus fulgidus |
| 8 | - |
assay at | Staphylococcus epidermidis |
| 8.5 | - |
assay at | Populus trichocarpa |
| 8.8 | - |
assay at | Pseudomonas putida |
| 8.8 | - |
assay at | Toxoplasma gondii |
| 8.8 | - |
shikimate oxidation assay at | Arabidopsis thaliana |
| 9 | - |
assay at | Escherichia coli |
| 9 | - |
assay at | Aquifex aeolicus |
| 9 | - |
assay at | Corynebacterium glutamicum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 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
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | cofactor binding might trigger domain movement | Staphylococcus epidermidis | |
| NADP+ | dependent on | Staphylococcus aureus | |
| NADP+ | dependent on | Escherichia coli | |
| NADP+ | dependent on | Mycobacterium tuberculosis | |
| NADP+ | dependent on | Helicobacter pylori | |
| NADP+ | dependent on | Aquifex aeolicus | |
| NADP+ | dependent on | Pseudomonas putida | |
| NADP+ | dependent on | Aspergillus nidulans | |
| NADP+ | dependent on | Archaeoglobus fulgidus | |
| NADP+ | dependent on | Corynebacterium glutamicum | |
| NADP+ | dependent on | Staphylococcus epidermidis | |
| NADP+ | dependent on | Toxoplasma gondii | |
| NADPH | dependent on | Staphylococcus aureus | |
| NADPH | dependent on | Escherichia coli | |
| NADPH | dependent on | Mycobacterium tuberculosis | |
| NADPH | dependent on | Helicobacter pylori | |
| NADPH | dependent on | Aquifex aeolicus | |
| NADPH | dependent on | Pseudomonas putida | |
| NADPH | dependent on | Aspergillus nidulans | |
| NADPH | dependent on | Archaeoglobus fulgidus | |
| NADPH | dependent on | Corynebacterium glutamicum | |
| NADPH | dependent on | Staphylococcus epidermidis | |
| NADPH | dependent on | Toxoplasma gondii | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| metabolism | the enzyme catalyze the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Toxoplasma gondii |
| metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Staphylococcus aureus |
| metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Escherichia coli |
| metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Mycobacterium tuberculosis |
| metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Helicobacter pylori |
| metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Aquifex aeolicus |
| metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Pseudomonas putida |
| metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Archaeoglobus fulgidus |
| metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Corynebacterium glutamicum |
| metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Staphylococcus epidermidis |
| 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 |
| 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 DHQSDH 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 |
| 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 DHQSDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQSDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processes | Populus trichocarpa |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
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Release 2023.1 (January 2023)
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