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Information on EC 5.4.99.5 - chorismate mutase and Organism(s) Escherichia coli and UniProt Accession P0A9J8

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.5 chorismate mutase
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Escherichia coli
UNIPROT: P0A9J8 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
chorismate mutase, p-protein, chorismate mutase/prephenate dehydratase, chorismate mutase-prephenate dehydrogenase, bacillus subtilis chorismate mutase, cm type 2, rv1885c, cm0819, atcm1, chorismate mutase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chorismate mutase
-
-
chorismate mutase-prephenate dehydrogenase
-
bifunctional enzyme
Chorismate mutase/prephenate dehydratase
CM-prephenate dehydratase
-
bifunctional enzyme
CM-TyrAp
-
bifunctional enzyme
CM/PDT
-
bi-functional chorismate mutase/prephenate dehydratase
Mutase, chorismate
-
-
-
-
P protein
-
-
-
-
P-protein
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
rearrangement
Claisen rearrangement
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Chorismate pyruvatemutase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9068-30-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Chorismate
Prephenate
show the reaction diagram
Chorismate
?
show the reaction diagram
Chorismate
Prephenate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Chorismate
Prephenate
show the reaction diagram
Chorismate
?
show the reaction diagram
Chorismate
Prephenate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
enhances activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2S,3S,5S,7S)-10-hydroxy-3-oxo-2-oxa-5-azatricyclo[4.3.1.1(4,8)]undecane-8-carboxylate
-
does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
-
(1R,3R,5S,8R)-2-azatricyclo[3.3.1.0(1,8)]-non-6-ene-3,5-dicarboxylate
-
exo arizidine analogue, no time-dependent loss of activity is observed in the presence of this potentially reactive aza inhibitor
(1R,3R,5S,8S)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylate
-
does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
(1R,3S,5S,8S)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylate
-
does not display tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than the ether analogue
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
-
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
-
(1S,4S,6R,8S,10S)-3-oxo-5-aza-2-oxa-tetracyclo[4.3.1.(4,8).0(6,10)]undecane-8-carboxylate
-
tetracyclic lactone, no time-dependent loss of activity is observed in the presence of this potentially reactive aza inhibitor
(2E)-8-exo-3-Hydroximino-8-hydroxy-2-oxabicyclo-[3.3.1]non-6-ene-5-carboxylic acid
-
poor
3-endo,6-exo-6-Hydroxy-7-bicyclo[3.3.1]-nonene-1,3-dicarboxylic acid
-
poor
3-endo,8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
potent
5,5'-dithiobis(2-nitrobenzoate)
-
-
8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]nona-3,6-diene-3,5-dicarboxylic acid
-
slight
iodoacetamide
-
-
NaCl
-
inhibition is cooperative, NaCl also increases the sensitivity of the enzyme to inhibition by Phe
prephenate
Transition state analogue inhibitor
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 0.669
chorismate
0.04 - 2.547
chorismate
0.47 - 1
prephenate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33.4 - 50.77
chorismate
0.00983 - 366000
chorismate
94100 - 94140
prephenate
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
30°C, pH 7.5, chorismate mutase domain of P-protein
0.0076
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
30°C, pH 7.5, chorismate mutase domain of P-protein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25790
gel filtration
39000
-
2 * 39000, SDS-PAGE
40000
42042
-
2 * 42042, calculation from nucleotide sequence
78000
-
sedimentation equilibrium analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
alpha2, 2 * 11883-11887, deduced from amino acid sequence, ESI-MS, MALDI-MS
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A32S
increased catalytic efficiency
D48I
no activity
I81L/V85I
reduced catalytic efficiency, alters packing against the hydrophobic ring face of the reacting molecule
L7I
no significant effect on catalytic efficiency
V35I
increased KM and turnover values compared to wild type
DELTA102-285
-
hybrid of chorismate mutase and allosteric domain from P-protein without prephrenate dehydratase
H131A
-
30% activity compared to wild-type enzyme
H153N
-
lower turnover and higher KM than wild-type enzyme
H189N
-
much lower turnover than wild-type enzyme
H197N
-
lower turnover and higher KM than wild-type enzyme
H239N
-
lower turnover and higher KM than wild-type enzyme
H245N
-
lower turnover and higher KM than wild-type enzyme
H257A
-
lower turnover and higher KM than wild-type enzyme
H265A
-
lower turnover and higher KM than wild-type enzyme
H347N
-
lower turnover than wild-type enzyme
K37A
-
more poorly expressed than wild-type, inactive and instable
K37Q
-
no activity
K39N
-
the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme
K39Q
-
the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme
K39R
-
the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme
Q88R
-
the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63
midpoint of unfolding transitions
54
-
1 h, 50% loss of activity, wild-type enzyme
58
-
1 h, 50% inactivation, genetically engineered enzyme with amino acid residues 1-285
62
-
1 h, 50% inactivation, genetically engineered enzyme with amino acid residues 1-300
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stable in high concentrations of glycerol, above 10% v/v, pH 7.5-8.0, and in the presence of thiols, citrate, and NAD+
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-78°C, 100 mM N-ethylmorpholine, 1.0 mM dithioerythritol, 1.0 mM N-ethylene-diaminetetraacetic acid, 21 mM trisodium citrate, 10% (v/v) glycerol in doubly distilled water adjusted to pH 7.0 with concentrated HCl
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminal Met1 is in most samples removed
chorismate mutase/prephenate dehydratase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
expressed in Arabidopsis thaliana
-
expressed in Escherichia coli strain FA114
-
expression in Escherichia coli
-
generation of transgenic Arabidopsis plants expressing a bacterial feedback-insensitive chorismate mutase/prephenate dehydratase gene (truncated PheA) under the control of the 35S CaMV promoter, fused inframe at the 3' end of the coding sequence to DNA encoding a hemagglutinin epitope tag. Two chimeric constructs: in one, DNA encoding a Rubisco small subunit-3A plastid transit peptide is fused in-frame to the 5' end of the PheA open reading frame to direct the bacterial enzyme in to the plastid where aromatic amino acid biosynthesis is localized. The second construct lacks the Rubisco small subunit-3A plastid transit peptide in order to test whether aromatic amino acid metabolism is strictly localized to the plastid or whether at least some parts of it operate in the cytosol. Both constructs transformed into Arabidopsis plants, and homozygous T2 plants are generated
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
misfolded, higher-order aggregates convert into fully active dimeric protein by denaturation with guanidinium chloride and subsequent renaturation upon dilution into native buffer
refolding after treatment with urea
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
As an intramolecular reaction that appears to be catalyzed without intermediate steps, covalent catalysis, or modification of the reaction pathway, the chorismate-prephenate rearrangement has become an important model system for theoretical approaches to the study of enzyme catalysis
synthesis
synthesis of L-phenylalanine (an important amino acid that is widely used in the production of food flavors and pharmaceuticals) by engineered Escherichia coli. Coexpression of Vitreoscilla hemoglobin gene, driven by a tac promoter, with the genes encoding 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (aroF) and feedback-resistant chorismate mutase/prephenate dehydratase (pheAfbr), leads to increased productivity of L-phenylalanine and decreased demand for aeration by Escherichia coli CICC10245
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cotton, R.G.H.; Gibson, F.
The biosynthesis of phenylalanine and tyrosine enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase
Biochim. Biophys. Acta
100
76-88
1965
Klebsiella aerogenes, Escherichia coli
Manually annotated by BRENDA team
Gething, M.J.; Davidson, B.E.; Dopheide, T.A.A.
Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 1. The effect of NaCl and its use in a new purification involving affinity chromatography on sepharosyl-phenylalanine
Eur. J. Biochem.
71
317-325
1976
Escherichia coli
Manually annotated by BRENDA team
Gething, M.J.; Davidson, B.E.
Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 2. Evidence for identical subunits catalysing the two activities
Eur. J. Biochem.
71
327-336
1976
Escherichia coli
Manually annotated by BRENDA team
Hoare, J.H.; Berchtold, G.A.
Chorismate mutase-catalyzed reaction of (+/-)-chorismic acid
Biochem. Biophys. Res. Commun.
106
660-662
1982
Escherichia coli, Kitasatospora aureofaciens, Kitasatospora aureofaciens tue 24
Manually annotated by BRENDA team
Davidson, B.E.; Hudson, G.S.
Chorismate mutase-prephenate dehydrogenase from Escherichia coli
Methods Enzymol.
142
440-450
1987
Escherichia coli
Manually annotated by BRENDA team
Stewart, J.; Wilson, D.B.; Ganem, B.
Chorismate mutase/prephenate dehydratase from Escherichia coli: subcloning, overproduction and purification
Tetrahedron
47
2573-2577
1991
Escherichia coli
-
Manually annotated by BRENDA team
Bartlett, P.A.; Nakagawa, Y.; Johnson, C.R.; Reich, S.H.; Luis, A.
Chorismate mutase inhibitors: synthesis and evaluation of some potential transition-state analogues
J. Org. Chem.
53
3195-3210
1988
Escherichia coli
-
Manually annotated by BRENDA team
Stewart, J.; Wilson, D.B.; Ganem, B.
A genetically engineered monofunctional chorismate mutase
J. Am. Chem. Soc.
112
4582-4584
1990
Escherichia coli
-
Manually annotated by BRENDA team
Lee, A.Y.; Zhang, S.; Kongsaeree, P.; Clardy, J.; Ganem, B.; Erickson,J.W.; Xie, D.
Thermodynamics of a transition state analogue inhibitor binding to Escherichia coli chorismate mutase: probing the charge state of an active site residue and its role in inhibitor binding and catalysis
Biochemistry
37
9052-9057
1998
Escherichia coli
Manually annotated by BRENDA team
Hertel, S.C.; Hieke, M.; Grger, D.
Purification and characterization of chorismate mutase isoenzymes from Ruta graveolens
Acta Biotechnol.
11
39-48
1991
Escherichia coli, Ruta graveolens
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Zhang, S.; Kongaeree, P.; Clardy, J.; Wilson, D.B.; Ganem, B.
Site-directed mutagenesis of monofunctional chorismate mutase engineered from the E. coli P-protein
Bioorg. Med. Chem.
4
1015-1020
1996
Escherichia coli
Manually annotated by BRENDA team
Zhang, S.; Pohnert, G.; Kongsaeree, P.; Wilson, D.B.; Clardy, J.; Ganem, B.
Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins
J. Biol. Chem.
273
6248-6253
1998
Escherichia coli
Manually annotated by BRENDA team
Davidson, B.E.
Chorismate mutase-prephenate dehydratase from Escherichia coli
Methods Enzymol.
142
432-439
1987
Klebsiella aerogenes, Cupriavidus necator, Escherichia coli, Pseudomonas sp., Salmonella enterica subsp. enterica serovar Typhimurium, Xanthomonas campestris
Manually annotated by BRENDA team
Christendat, D.; Saridakis, V.C.; Turnbull, J.L.
Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli
Biochemistry
37
15703-15712
1998
Escherichia coli
Manually annotated by BRENDA team
MacBeath, G.; Kast, P.; Hilvert, D.
A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii
Biochemistry
37
10062-10073
1998
Methanocaldococcus jannaschii, Escherichia coli (P0A9J8), Escherichia coli
Manually annotated by BRENDA team
Zhang, S.; Wilson, D.B.; Ganem, B.
An engineered chorismate mutase with allosteric regulation
Bioorg. Med. Chem.
11
3109-3114
2003
Escherichia coli
Manually annotated by BRENDA team
Mandal, A.; Hilvert, D.
Charge optimization increases the potency and selectivity of a chorismate mutase inhibitor
J. Am. Chem. Soc.
125
5598-5599
2003
Bacillus subtilis, Escherichia coli
Manually annotated by BRENDA team
Zhang, X.; Zhang, X; Bruice, T.C.
A definitive mechanism for chorismate mutase
Biochemistry
44
10443-10448
2005
Escherichia coli (P0A9J8), Escherichia coli
Manually annotated by BRENDA team
Hediger, M.E.
Design, synthesis, and evaluation of aza inhibitors of chorismate mutase
Bioorg. Med. Chem.
12
4995-5010
2004
Escherichia coli, Escherichia coli JFM-30
Manually annotated by BRENDA team
Lassila, J.K.; Keeffe, J.R.; Oelschlaeger, P.; Mayo, S.L.
Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity
Protein Eng. Des. Sel.
18
161-163
2005
Escherichia coli (P0A9J8), Escherichia coli
Manually annotated by BRENDA team
Lassila, J.K.; Keeffe, J.R.; Kast, P.; Mayo, S.L.
Exhaustive mutagenesis of six secondary active-site residues in Escherichia coli chorismate mutase shows the importance of hydrophobic side chains and a helix N-capping position for stability and catalysis
Biochemistry
46
6883-6891
2007
Escherichia coli (P0A9J8), Escherichia coli
Manually annotated by BRENDA team
Chavez-Bejar, M.I.; Lara, A.R.; Lopez, H.; Hernandez-Chavez, G.; Martinez, A.; Ramirez, O.T.; Bolivar, F.; Gosset, G.
Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis
Appl. Environ. Microbiol.
74
3284-3290
2008
Escherichia coli, Escherichia coli JM101
Manually annotated by BRENDA team
Tzin, V.; Malitsky, S.; Aharoni, A.; Galili, G.
Expression of a bacterial bi-functional chorismate mutase/prephenate dehydratase modulates primary and secondary metabolism associated with aromatic amino acids in Arabidopsis
Plant J.
60
156-167
2009
Escherichia coli
Manually annotated by BRENDA team
Wu, W.B.; Guo, X.L.; Zhang, M.L.; Huang, Q.G.; Qi, F.; Huang, J.Z.
Enhancement of L-phenylalanine production in Escherichia coli by heterologous expression of Vitreoscilla hemoglobin
Biotechnol. Appl. Biochem.
65
476-483
2018
Escherichia coli (C7EXK8), Escherichia coli
Manually annotated by BRENDA team