Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.4.99.5 extracted from

  • Kroll, K.; Holland, C.K.; Starks, C.M.; Jez, J.M.
    Evolution of allosteric regulation in chorismate mutases from early plants (2017), Biochem. J., 474, 3705-3717 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
cysteine
-
Arabidopsis thaliana
histidine
-
Arabidopsis thaliana
histidine is a positive effector for the enzyme Physcomitrium patens
histidine is a positive effector for the enzyme Amborella trichopoda
additional information isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine Arabidopsis thaliana
additional information neither tyrosine nor phenylalanine alters the activity of enzyme SmCM Selaginella moellendorffii
tryptophan
-
Arabidopsis thaliana
tryptophan is a positive effector for the enzyme Physcomitrium patens
tryptophan is a positive effector for the enzyme Selaginella moellendorffii
tryptophan is a positive effector for the enzyme Amborella trichopoda
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)

Cloned (Comment) Organism
sequence comparisons Arabidopsis thaliana
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3) Physcomitrium patens
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3) Selaginella moellendorffii
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3) Amborella trichopoda

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
additional information neither tyrosine nor phenylalanine alters the activity of enzyme SmCM Selaginella moellendorffii
tyrosine is a negative effector for the enzyme; is a negative effector for the enzyme Amborella trichopoda
tyrosine is a negative effector for the enzyme; is a negative effector for the enzyme Physcomitrium patens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten steady-state kinetics Physcomitrium patens
additional information
-
additional information Michaelis-Menten steady-state kinetics Selaginella moellendorffii
additional information
-
additional information Michaelis-Menten steady-state kinetics Amborella trichopoda
2.33
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Physcomitrium patens
2.39
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Physcomitrium patens
3.19
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Amborella trichopoda
5.19
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Selaginella moellendorffii
6.79
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Amborella trichopoda

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Arabidopsis thaliana 9507
-
chloroplast identification of a chloroplast transit peptide Physcomitrium patens 9507
-
chloroplast identification of a chloroplast transit peptide Amborella trichopoda 9507
-
cytosol
-
Arabidopsis thaliana 5829
-
additional information enzyme SmCM is not predicted to have a chloroplast signal peptide Selaginella moellendorffii
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
about, recombinant detagged enzyme, gel filtration Physcomitrium patens
60000
-
about, recombinant detagged enzyme, gel filtration Selaginella moellendorffii
60000
-
about, recombinant detagged enzyme, gel filtration Amborella trichopoda

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Chorismate Physcomitrium patens
-
Prephenate
-
?
Chorismate Selaginella moellendorffii
-
Prephenate
-
?
Chorismate Amborella trichopoda
-
Prephenate
-
?
Chorismate Arabidopsis thaliana
-
Prephenate
-
?

Organism

Organism UniProt Comment Textmining
Amborella trichopoda U5D896
-
-
Amborella trichopoda W1PFX5
-
-
Arabidopsis thaliana P42738
-
-
Arabidopsis thaliana Q9C544
-
-
Arabidopsis thaliana Q9S7H4
-
-
Physcomitrium patens A0A2K1JMA3
-
-
Physcomitrium patens A9S498
-
-
Selaginella moellendorffii D8R1Y1
-
-

Purification (Commentary)

Purification (Comment) Organism
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
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
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]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
enzyme activity in presence of amino acid effectors, overview Physcomitrium patens
additional information
-
enzyme activity in presence of amino acid effectors, overview Selaginella moellendorffii
additional information
-
enzyme activity in presence of amino acid effectors, overview Amborella trichopoda

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
-
Physcomitrium patens Prephenate
-
?
Chorismate
-
Selaginella moellendorffii Prephenate
-
?
Chorismate
-
Amborella trichopoda Prephenate
-
?
Chorismate
-
Arabidopsis thaliana Prephenate
-
?
Chorismate interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate Physcomitrium patens Prephenate
-
?
Chorismate interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate Selaginella moellendorffii Prephenate
-
?
Chorismate interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate Amborella trichopoda Prephenate
-
?
Chorismate interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate Arabidopsis thaliana Prephenate
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE Physcomitrium patens
homodimer 2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE Selaginella moellendorffii
homodimer 2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE Amborella trichopoda

Synonyms

Synonyms Comment Organism
AmtCM1
-
Amborella trichopoda
AmtCM2
-
Amborella trichopoda
AtCM1
-
Arabidopsis thaliana
AtCM2
-
Arabidopsis thaliana
AtCM3
-
Arabidopsis thaliana
PpCM1
-
Physcomitrium patens
PpCM2
-
Physcomitrium patens
SmCM
-
Selaginella moellendorffii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Arabidopsis thaliana
15
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Amborella trichopoda
16
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Arabidopsis thaliana
18.8
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Selaginella moellendorffii
19.5
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Physcomitrium patens
20.7
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Physcomitrium patens
22.8
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Amborella trichopoda
39
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Physcomitrium patens
8
-
assay at Selaginella moellendorffii
8
-
assay at Amborella trichopoda
8
-
assay at Arabidopsis thaliana

Expression

Organism Comment Expression
Amborella trichopoda the isozyme AtmCM2 is downregulated by phenylalanine down

General Information

General Information Comment Organism
evolution analysis of evolution of allosteric regulation in plant chorismate mutases Arabidopsis thaliana
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
evolution evolution of allosteric regulation in plant chorismate mutases, overview Physcomitrium patens
evolution evolution of allosteric regulation in plant chorismate mutases, overview Selaginella moellendorffii
evolution evolution of allosteric regulation in plant chorismate mutases, overview Amborella trichopoda
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
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
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
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
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
additional information structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview Physcomitrium patens
additional information structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview Selaginella moellendorffii
additional information structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview Amborella trichopoda
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
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
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
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
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
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]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.36
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Amborella trichopoda
3.62
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Selaginella moellendorffii
4.7
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Amborella trichopoda
8.34
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Physcomitrium patens
8.66
-
chorismate pH 8.0, temperature not specified in the publication, recombinant enzyme Physcomitrium patens