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(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
NaCl
-
inhibition is cooperative, NaCl also increases the sensitivity of the enzyme to inhibition by Phe
Transition state analogue inhibitor
-
-
-
prephenate
-
competitive
prephenate
-
competitive inhibition
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additional information
additional information
-
0.22
chorismate
mutant A32S
0.249
chorismate
mutant L7I
0.304
chorismate
wild type
0.365
chorismate
mutant V35I
0.669
chorismate
mutant I81L/V85I
0.04
chorismate
-
in presence of NAD+
0.041
chorismate
-
30°C, pH 7.2, mutant H347N
0.045
chorismate
-
30°C, pH 7.2, wild-type
0.051
chorismate
-
30°C, pH 7.2, mutant H153N
0.053
chorismate
-
30°C, pH 7.2, mutant H131A
0.068
chorismate
-
30°C, pH 7.2, mutant H197N
0.092
chorismate
-
pH 7.5, in absence of NAD+
0.098
chorismate
-
30°C, pH 7.2, mutant H257A
0.099
chorismate
-
30°C, pH 7.2, mutant H265A
0.126
chorismate
-
30°C, pH 7.2, mutant H239N
0.225
chorismate
-
30°C, pH 7.2, mutant H245N
0.226
chorismate
-
37°C, pH 7.8, in presence of P-protein
0.29
chorismate
-
genetically engineered monofunctional chorismate mutase that contains only 109 amino acids
0.296
chorismate
-
37°C, pH 7.8
0.3
chorismate
-
wild-type enzyme
0.39
chorismate
-
chorismate mutase domain of P-protein
0.45
chorismate
-
mutant enzyme Lys39Asn
0.59
chorismate
-
mutant enzyme Lys39Arg
0.59 - 1
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine
0.628
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine
1.036
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine
1.16
chorismate
-
mutant enzyme Lys39Gln
2.547
chorismate
-
37°C, pH 7.8, DELTA102-285
0.47 - 1
prephenate
-
-
0.549
prephenate
-
37°C, pH 7.8, in presence of P-protein
additional information
additional information
The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-
additional information
additional information
-
The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-
additional information
additional information
-
when the pH increases from pH 6.2 to pH 8.6 the Km-values for prephenate and chorismate increase substantially
-
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0.00983 - 366000
chorismate
additional information
additional information
-
33.4
chorismate
mutant I81L/V85I
36.55
chorismate
mutant L7I
38.87
chorismate
wild type
45.13
chorismate
mutant A32S
50.77
chorismate
mutant V35I
0.00983
chorismate
-
mutant enzyme Lys39Arg
0.0492
chorismate
-
mutant enzyme Lys39Asn
0.123
chorismate
-
mutant enzyme Lys39Arg
2.3
chorismate
-
30°C, pH 7.2, mutant H239N
4.8
chorismate
-
30°C, pH 7.2, mutant H245N
6
chorismate
-
30°C, pH 7.2, mutant H347N
7.2
chorismate
-
30°C, pH 7.2, mutant H131A
8
chorismate
-
30°C, pH 7.2, mutant H257A
10
chorismate
-
30°C, pH 7.2, mutant H153N
15
chorismate
-
30°C, pH 7.2, mutant H265A
16
chorismate
-
30°C, pH 7.2, mutant H197N
27
chorismate
-
30°C, pH 7.2, wild-type
39
chorismate
-
wild-type enzyme
40.7
chorismate
-
genetically engineered enzyme containg the amino acid residues 1-300
41.4
chorismate
-
wild-type enzyme
44.3
chorismate
-
genetically engineered enzyme containg the amino acid residues 1-285
64
chorismate
-
chorismate mutase domain of P-protein
140500
chorismate
-
37°C, pH 7.8, in presence of P-protein
141000
chorismate
-
37°C, pH 7.8, in presence of P-protein
148900
chorismate
-
37°C, pH 7.8, chorismate mutase
149000
chorismate
-
37°C, pH 7.8, chorismate mutase
234000
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine
234100
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine
253000
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine
253400
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine
257900
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine
258000
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine
365600
chorismate
-
37°C, pH 7.8, DELTA102-285
366000
chorismate
-
37°C, pH 7.8, DELTA102-285
94100
prephenate
-
37°C, pH 7.8, in presence of P-protein
94140
prephenate
-
37°C, pH 7.8, in presence of P-protein
additional information
additional information
The kcat of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-
additional information
additional information
-
The kcat of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
turnover of mutant H189N enzyme is lower than 0.0025 per second
additional information
additional information
-
turnover of mutant H189N enzyme is lower than 0.0025 per second
-
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A32S
increased catalytic efficiency
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
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
Q88E
-
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
Q88E
-
mutation of Gln88 to Glu in the monofunctional chorismate mutase results in an enzyme with a pH profile of activity significantly different from that of the wild-type protein
additional information
EcCM active-site residues (Leu7, Ala32, Val35, Asp48, Ile81, Val85) that mutated in our previous computational design experiment. Each of the 114 variants tested for complementation of the chorismate mutase deficiency of the auxotrophic Escherichia coli KA12/pKIMP-UAUC system. 34% of all single mutants are scored as biological active
additional information
-
EcCM active-site residues (Leu7, Ala32, Val35, Asp48, Ile81, Val85) that mutated in our previous computational design experiment. Each of the 114 variants tested for complementation of the chorismate mutase deficiency of the auxotrophic Escherichia coli KA12/pKIMP-UAUC system. 34% of all single mutants are scored as biological active
additional information
-
proteins containing residues 1-285 and residues 1-300 retain full chorismate mutase activity and prephenate dehydratase activity, but exhibit no feedback inhibition. Proteins containing residues 101-386 and residues 101-300 retain full prephenate dehydratase activity, but lack mutase activity
additional information
-
genetically engineered monofunctional chorismate mutase that contains only 109 amino acids starting with the bifunctional P protein that also exhibits prephenate dehydratase activity and is composed of 386 amino acids
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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
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1965
Klebsiella aerogenes, Escherichia coli
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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
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Escherichia coli
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Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 2. Evidence for identical subunits catalysing the two activities
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71
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Escherichia coli
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Chorismate mutase-catalyzed reaction of (+/-)-chorismic acid
Biochem. Biophys. Res. Commun.
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1982
Escherichia coli, Kitasatospora aureofaciens, Kitasatospora aureofaciens tue 24
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Chorismate mutase-prephenate dehydrogenase from Escherichia coli
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Escherichia coli
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Chorismate mutase/prephenate dehydratase from Escherichia coli: subcloning, overproduction and purification
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47
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Escherichia coli
-
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Chorismate mutase inhibitors: synthesis and evaluation of some potential transition-state analogues
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53
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Escherichia coli
-
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A genetically engineered monofunctional chorismate mutase
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112
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Escherichia coli
-
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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
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37
9052-9057
1998
Escherichia coli
brenda
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Purification and characterization of chorismate mutase isoenzymes from Ruta graveolens
Acta Biotechnol.
11
39-48
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Escherichia coli, Ruta graveolens
-
brenda
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
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334
233-236
1993
Arabidopsis thaliana, Escherichia coli
brenda
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
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4
1015-1020
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Escherichia coli
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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
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273
6248-6253
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Escherichia coli
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Chorismate mutase-prephenate dehydratase from Escherichia coli
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142
432-439
1987
Klebsiella aerogenes, Cupriavidus necator, Escherichia coli, Pseudomonas sp., Salmonella enterica subsp. enterica serovar Typhimurium, Xanthomonas campestris
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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
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37
15703-15712
1998
Escherichia coli
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MacBeath, G.; Kast, P.; Hilvert, D.
A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii
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37
10062-10073
1998
Methanocaldococcus jannaschii, Escherichia coli (P0A9J8), Escherichia coli
brenda
Zhang, S.; Wilson, D.B.; Ganem, B.
An engineered chorismate mutase with allosteric regulation
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11
3109-3114
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Escherichia coli
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Mandal, A.; Hilvert, D.
Charge optimization increases the potency and selectivity of a chorismate mutase inhibitor
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125
5598-5599
2003
Bacillus subtilis, Escherichia coli
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Zhang, X.; Zhang, X; Bruice, T.C.
A definitive mechanism for chorismate mutase
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44
10443-10448
2005
Escherichia coli (P0A9J8), Escherichia coli
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Design, synthesis, and evaluation of aza inhibitors of chorismate mutase
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12
4995-5010
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Escherichia coli, Escherichia coli JFM-30
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Lassila, J.K.; Keeffe, J.R.; Oelschlaeger, P.; Mayo, S.L.
Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity
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18
161-163
2005
Escherichia coli (P0A9J8), Escherichia coli
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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
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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
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74
3284-3290
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Escherichia coli, Escherichia coli JM101
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Expression of a bacterial bi-functional chorismate mutase/prephenate dehydratase modulates primary and secondary metabolism associated with aromatic amino acids in Arabidopsis
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60
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Escherichia coli
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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
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65
476-483
2018
Escherichia coli (C7EXK8), Escherichia coli
brenda