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Information on EC 5.4.99.5 - chorismate mutase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9C544
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EC Tree
5.4.99.5 chorismate mutaseSpecify your search results
Word Map
- 5.4.99.5
- shikimate
-
sieve
-
monofunctional
- phloem
- l-phenylalanine
- l-tyrosine
- 7-phosphate
- mutases
-
t-proteins
-
3-deoxy-d-arabino-heptulosonate
- phenylpyruvate
-
claisen
- arogenate
-
pericyclic
-
nonketotic
- hyperglycinemia
- isochorismate
-
cyclohexadienyl
- hydroxyphenylpyruvate
-
photorespiratory
-
preorganization
- drug development
-
3-deoxy-d-arabino-heptulosonate-7-phosphate
- meloidogyne
- synthesis
- agriculture
- analysis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
chorismate mutase, p-protein, chorismate mutase/prephenate dehydratase, chorismate mutase-prephenate dehydrogenase, bacillus subtilis chorismate mutase, cm type 2, cm0819, atcm1, rv1885c, chorismate mutase 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Chorismate mutase/prephenate dehydratase
-
-
-
-
Mutase, chorismate
-
-
-
-
P protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
Chorismate pyruvatemutase
-
CAS REGISTRY NUMBER
COMMENTARY
9068-30-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Chorismate
Prephenate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
-
-
?
Chorismate
?
-
catalyzes the first step in the branch of the shikimate pathway which leads to the aromatic amino acids, Phe and Tyr
-
-
?
Chorismate
?
-
the existence of a cytosolic isoenzyme in addition to the plastidic isoenzyme implies that either a cytosolic pathway, partial or complete, for the biosynthesis of Phe and Tyr exists, or that prephenate, originating from chorismate in the cytosol, is utilized for the synthesis of metabolites other than these two aromatic amino acids
-
-
?
Chorismate
?
-
plastidic isoenzyme is elicitor-inducible and pathogen-inducible
-
-
?
Chorismate
Prephenate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Chorismate
?
-
catalyzes the first step in the branch of the shikimate pathway which leads to the aromatic amino acids, Phe and Tyr
-
-
?
Chorismate
?
-
the existence of a cytosolic isoenzyme in addition to the plastidic isoenzyme implies that either a cytosolic pathway, partial or complete, for the biosynthesis of Phe and Tyr exists, or that prephenate, originating from chorismate in the cytosol, is utilized for the synthesis of metabolites other than these two aromatic amino acids
-
-
?
Chorismate
?
-
plastidic isoenzyme is elicitor-inducible and pathogen-inducible
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenylalanine
model of the AtCM1x02phenylalanine complex including residues Arg79-Val290 and Val307-Asp340, the phenylalanine ligand, and 83 waters, inhibits about 20fold
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
-
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
-
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
-
additional information
isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine
-
additional information
isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine
-
additional information
isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.15
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.55
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
additional information
additional information
steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site
-
additional information
additional information
steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site
-
additional information
additional information
steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site
-
additional information
additional information
-
steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site
-
additional information
additional information
steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview
-
additional information
additional information
steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview
-
additional information
additional information
steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview
-
additional information
additional information
-
steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview
-
additional information
additional information
steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics
-
additional information
additional information
-
steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
13
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
16
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
16.1
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
38.7
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
39
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.8
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
29.27
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
258
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
analysis of evolution of allosteric regulation in plant chorismate mutases
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
physiological function
evolution
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
physiological function
additional information
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
physiological function
isozyme AtCM3 is alosterically regulated
evolution
analysis of evolution of allosteric regulation in plant chorismate mutases
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
physiological function
AtCM2 is a nonallosteric form
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
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
physiological function
isozyme AtCM1 is alosterically regulated
additional information
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
-
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
-
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CM3_ARATH
316
0
36570
Swiss-Prot
Chloroplast (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged wild-type enzyme in complex with phenylalanine or tyrosine, hanging drop vapordiffusion method, mixing 0f 0.001 ml of 9 mg/ml protein in 25 mM HEPES, pH 7.5, and 100 mM NaCl, with 0.001 ml of reservoir solution containing 30% PEG 400, 0.1 M HEPES, pH 7.5, 0.2 M MgCl2, and 1 mM of either phenylalanine or tyrosine, X-ray diffraction structure determination and analysis at 2.30-2.45 A resolution, molecular replacement using yeast chorismate mutase structure, PDB ID 4CSM, as a search model
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D132G
site-directed mutagenesis, the mutant enzyme kinetically resembles isozyme AtCM1, it retains activation by tryptophan, although to a lesser extent than observed with wild-type AtCM3
G149A
site-directed mutagenesis, the mutation eliminates the effector action of both phenylalanine and tyrosine
G149D
site-directed mutagenesis, the mutation eliminates the effector action of both phenylalanine and tyrosine
G213A
site-directed mutagenesis, mutation in effector binding site, the mutation eliminates the effect of aromatic amino acids on enzymatic activity
G213P
site-directed mutagenesis, mutation in effector binding site, the mutation eliminates the effect of aromatic amino acids on enzymatic activity
H145Q
site-directed mutagenesis, mutation in effector binding site, the mutation has varyring effects on the EC50 values for the aromatic amino acid effectors but does not change either positive or negative effects on enzymatic activity
R79k
site-directed mutagenesis, mutation in effector binding site, the mutation has varyring effects on the EC50 values for the aromatic amino acid effectors but does not change either positive or negative effects on enzymatic activity
V217T
site-directed mutagenesis, mutation in effector binding site
additional information
additional information
generation of the expression construct N-terminally hexahistidine-tagged AtCM1 lacking the plastid localization peptide, AtCM1DELTA66
additional information
generation of the expression construct N-terminally hexahistidine-tagged AtCM1 lacking the plastid localization peptide, AtCM1DELTA66
additional information
generation of the expression construct N-terminally hexahistidine-tagged AtCM1 lacking the plastid localization peptide, AtCM1DELTA66
additional information
-
generation of the expression construct N-terminally hexahistidine-tagged AtCM1 lacking the plastid localization peptide, AtCM1DELTA66
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, benzamidine/nickel affinity chromatography, and gel filtration
AtCM1, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta II (DE3)
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, benzamidine/nickel affinity chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtCM3, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta II (DE3)
AtCM1, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta II (DE3)
recombinant His6-tagged wild-type enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, benzamidine/nickel affinity chromatography, and gel filtration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eberhard, J.; Ehrler, T.T.; Epple, P.; Felix, G.; Raesecke, H.R.; Amrhein, N.; Schmid, J.
Cytosolic and plastidic chorismate mutase isoenzymes from Arabidopsis thaliana: molecular characterization and enzymatic properties
Plant J.
10
815-821
1996
Arabidopsis thaliana
Eberhard, J.; Raesecke, H.R.; Schmid, J.; Amrhein, N.
Cloning and expression in yeast of a higher plant chorismate mutase. Molecular cloning, sequencing of the cDNA and characterization of the Arabidopsis thaliana enzyme expressed in yeast
FEBS Lett.
334
233-236
1993
Arabidopsis thaliana, Escherichia coli
Kroll, K.; Holland, C.K.; Starks, C.M.; Jez, J.M.
Evolution of allosteric regulation in chorismate mutases from early plants
Biochem. J.
474
3705-3717
2017
Physcomitrium patens (A0A2K1JMA3), Physcomitrium patens (A9S498), Selaginella moellendorffii (D8R1Y1), Arabidopsis thaliana (P42738), Arabidopsis thaliana (Q9C544), Arabidopsis thaliana (Q9S7H4), Amborella trichopoda (U5D896), Amborella trichopoda (W1PFX5)
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