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Literature summary extracted from
- Evolution of allosteric regulation in chorismate mutases from early plants (2017), Biochem. J., 474, 3705-3717 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.5 | cysteine | - |
Arabidopsis thaliana |  |
| 5.4.99.5 | histidine | - |
Arabidopsis thaliana | |
| 5.4.99.5 | histidine | is a positive effector for the enzyme | Physcomitrium patens | |
| 5.4.99.5 | histidine | is a positive effector for the enzyme | Amborella trichopoda | |
| 5.4.99.5 | additional information | isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine | Arabidopsis thaliana | |
| 5.4.99.5 | additional information | neither tyrosine nor phenylalanine alters the activity of enzyme SmCM | Selaginella moellendorffii | |
| 5.4.99.5 | tryptophan | - |
Arabidopsis thaliana | |
| 5.4.99.5 | tryptophan | is a positive effector for the enzyme | Physcomitrium patens | |
| 5.4.99.5 | tryptophan | is a positive effector for the enzyme | Selaginella moellendorffii | |
| 5.4.99.5 | tryptophan | is a positive effector for the enzyme | Amborella trichopoda | |
| 5.4.99.5 | tryptophan | is a positive effector for the enzyme, identification of the allosteric effector site and the structural differences between the R- (more active) and T-state (less active) forms of plant chorismate mutase | Physcomitrium patens | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.4.99.5 | sequence comparisons | Arabidopsis thaliana |
| 5.4.99.5 | sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3) | Physcomitrium patens |
| 5.4.99.5 | sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3) | Selaginella moellendorffii |
| 5.4.99.5 | sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3) | Amborella trichopoda |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.4.99.5 | purified recombinant detagged isozyme PpCM1 in complex with tryptophan, hanging drop vapor diffusion method, mixing of 0.001 ml of 6 mg/ml proteinin 25 mM HEPES, pH 7.5, and 100 mM NaCl with 0.001 ml of reservoir solution containing 10% w/v PEG 4000, 20% v/v 2-propanol, and 100 mM HEPES, pH 7.5, at 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement using Arabidopsis thaliana isozyme AtCM1 in complex with tyrosine structure (PDB ID 4PPU) as search model, modeling | Physcomitrium patens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.5 | additional information | neither tyrosine nor phenylalanine alters the activity of enzyme SmCM | Selaginella moellendorffii | |
| 5.4.99.5 | tyrosine | is a negative effector for the enzyme; is a negative effector for the enzyme | Amborella trichopoda | |
| 5.4.99.5 | tyrosine | is a negative effector for the enzyme; is a negative effector for the enzyme | Physcomitrium patens | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.5 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Physcomitrium patens | |
| 5.4.99.5 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Selaginella moellendorffii | |
| 5.4.99.5 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics | Amborella trichopoda | |
| 5.4.99.5 | 2.33 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Physcomitrium patens | |
| 5.4.99.5 | 2.39 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Physcomitrium patens | |
| 5.4.99.5 | 3.19 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Amborella trichopoda | |
| 5.4.99.5 | 5.19 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Selaginella moellendorffii | |
| 5.4.99.5 | 6.79 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Amborella trichopoda | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 5.4.99.5 | chloroplast | - |
Arabidopsis thaliana | 9507 | - |
| 5.4.99.5 | chloroplast | identification of a chloroplast transit peptide | Physcomitrium patens | 9507 | - |
| 5.4.99.5 | chloroplast | identification of a chloroplast transit peptide | Amborella trichopoda | 9507 | - |
| 5.4.99.5 | cytosol | - |
Arabidopsis thaliana | 5829 | - |
| 5.4.99.5 | additional information | enzyme SmCM is not predicted to have a chloroplast signal peptide | Selaginella moellendorffii | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.5 | 60000 | - |
about, recombinant detagged enzyme, gel filtration | Physcomitrium patens |
| 5.4.99.5 | 60000 | - |
about, recombinant detagged enzyme, gel filtration | Selaginella moellendorffii |
| 5.4.99.5 | 60000 | - |
about, recombinant detagged enzyme, gel filtration | Amborella trichopoda |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.5 | Chorismate | Physcomitrium patens | - |
Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | Selaginella moellendorffii | - |
Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | Amborella trichopoda | - |
Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | Arabidopsis thaliana | - |
Prephenate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.5 | Amborella trichopoda | U5D896 | - |
- |
| 5.4.99.5 | Amborella trichopoda | W1PFX5 | - |
- |
| 5.4.99.5 | Arabidopsis thaliana | P42738 | - |
- |
| 5.4.99.5 | Arabidopsis thaliana | Q9C544 | - |
- |
| 5.4.99.5 | Arabidopsis thaliana | Q9S7H4 | - |
- |
| 5.4.99.5 | Physcomitrium patens | A0A2K1JMA3 | - |
- |
| 5.4.99.5 | Physcomitrium patens | A9S498 | - |
- |
| 5.4.99.5 | Selaginella moellendorffii | D8R1Y1 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.4.99.5 | recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration | Physcomitrium patens |
| 5.4.99.5 | recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration | Selaginella moellendorffii |
| 5.4.99.5 | recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration | Amborella trichopoda |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.5 | additional information | - |
enzyme activity in presence of amino acid effectors, overview | Physcomitrium patens |
| 5.4.99.5 | additional information | - |
enzyme activity in presence of amino acid effectors, overview | Selaginella moellendorffii |
| 5.4.99.5 | additional information | - |
enzyme activity in presence of amino acid effectors, overview | Amborella trichopoda |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.5 | Chorismate | - |
Physcomitrium patens | Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | - |
Selaginella moellendorffii | Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | - |
Amborella trichopoda | Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | - |
Arabidopsis thaliana | Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate | Physcomitrium patens | Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate | Selaginella moellendorffii | Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate | Amborella trichopoda | Prephenate | - |
? | |
| 5.4.99.5 | Chorismate | interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate | Arabidopsis thaliana | Prephenate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.99.5 | homodimer | 2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE | Physcomitrium patens |
| 5.4.99.5 | homodimer | 2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE | Selaginella moellendorffii |
| 5.4.99.5 | homodimer | 2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE | Amborella trichopoda |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.5 | AmtCM1 | - |
Amborella trichopoda |
| 5.4.99.5 | AmtCM2 | - |
Amborella trichopoda |
| 5.4.99.5 | AtCM1 | - |
Arabidopsis thaliana |
| 5.4.99.5 | AtCM2 | - |
Arabidopsis thaliana |
| 5.4.99.5 | AtCM3 | - |
Arabidopsis thaliana |
| 5.4.99.5 | PpCM1 | - |
Physcomitrium patens |
| 5.4.99.5 | PpCM2 | - |
Physcomitrium patens |
| 5.4.99.5 | SmCM | - |
Selaginella moellendorffii |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.5 | 13 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Arabidopsis thaliana | |
| 5.4.99.5 | 15 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Amborella trichopoda | |
| 5.4.99.5 | 16 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Arabidopsis thaliana | |
| 5.4.99.5 | 18.8 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Selaginella moellendorffii | |
| 5.4.99.5 | 19.5 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Physcomitrium patens | |
| 5.4.99.5 | 20.7 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Physcomitrium patens | |
| 5.4.99.5 | 22.8 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Amborella trichopoda | |
| 5.4.99.5 | 39 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Arabidopsis thaliana | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.5 | 8 | - |
assay at | Physcomitrium patens |
| 5.4.99.5 | 8 | - |
assay at | Selaginella moellendorffii |
| 5.4.99.5 | 8 | - |
assay at | Amborella trichopoda |
| 5.4.99.5 | 8 | - |
assay at | Arabidopsis thaliana |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 5.4.99.5 | Amborella trichopoda | the isozyme AtmCM2 is downregulated by phenylalanine | down |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.4.99.5 | evolution | analysis of evolution of allosteric regulation in plant chorismate mutases | Arabidopsis thaliana |
| 5.4.99.5 | evolution | analysis of evolution of allosteric regulation in plant chorismate mutases. Phylogentically, the AtCM3-like clade is found only in the Brassicaceae, which suggests a possible specialized role for this enzyme in those plants | Arabidopsis thaliana |
| 5.4.99.5 | evolution | evolution of allosteric regulation in plant chorismate mutases, overview | Physcomitrium patens |
| 5.4.99.5 | evolution | evolution of allosteric regulation in plant chorismate mutases, overview | Selaginella moellendorffii |
| 5.4.99.5 | evolution | evolution of allosteric regulation in plant chorismate mutases, overview | Amborella trichopoda |
| 5.4.99.5 | metabolism | anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid | Selaginella moellendorffii |
| 5.4.99.5 | metabolism | anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid | Amborella trichopoda |
| 5.4.99.5 | metabolism | anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid | Arabidopsis thaliana |
| 5.4.99.5 | metabolism | anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid buildup of the amino acid | Physcomitrium patens |
| 5.4.99.5 | additional information | isozyme PpCM1 structure-function analysis, structure comparisons, active site and allosteric effector sites of PpCM1, targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview | Physcomitrium patens |
| 5.4.99.5 | additional information | structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview | Physcomitrium patens |
| 5.4.99.5 | additional information | structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview | Selaginella moellendorffii |
| 5.4.99.5 | additional information | structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview | Amborella trichopoda |
| 5.4.99.5 | physiological function | chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen re-arrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview | Physcomitrium patens |
| 5.4.99.5 | physiological function | chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview | Selaginella moellendorffii |
| 5.4.99.5 | physiological function | chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview | Amborella trichopoda |
| 5.4.99.5 | physiological function | chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The cytosolic chorismate mutase isozyme AtCM2 is unregulated | Arabidopsis thaliana |
| 5.4.99.5 | physiological function | chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The plastid-localized chorismate mutase isozyme AtCM1 is allosterically regulated. The allosterically regulated chorismate mutases are repressed by tyrosine and phenylalanine and are activated by tryptophan. The aromatic amino acids bind an effector site on the enzyme and regulate the ability of chorismate to bind at the active site for catalysis | Arabidopsis thaliana |
| 5.4.99.5 | physiological function | chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The plastid-localized chorismate mutase isozyme AtCM3 is allosterically regulated. The allosterically regulated chorismate mutases are repressed by tyrosine and phenylalanine and are activated by tryptophan. The aromatic amino acids bind an effector site on the enzyme and regulate the ability of chorismate to bind at the active site for catalysis | Arabidopsis thaliana |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.5 | 3.36 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Amborella trichopoda | |
| 5.4.99.5 | 3.62 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Selaginella moellendorffii | |
| 5.4.99.5 | 4.7 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Amborella trichopoda | |
| 5.4.99.5 | 8.34 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Physcomitrium patens | |
| 5.4.99.5 | 8.66 | - |
chorismate | pH 8.0, temperature not specified in the publication, recombinant enzyme | Physcomitrium patens | |
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