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Information on EC 5.4.99.5 - chorismate mutase and Organism(s) Bacillus subtilis and UniProt Accession P19080
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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: Bacillus subtilis
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, rv1885c, cm0819, atcm1, chorismate mutase 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Chorismate mutase/prephenate dehydratase
-
-
-
-
Mutase, chorismate
-
-
-
-
P protein
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Chorismate = prephenate
The active site of the enzyme which is found in a pocket formed by two different chains is shown. Applying the TPS method of Chandler and co-workers to study the chorismate to prephenate reaction
Chorismate = prephenate
Wild-type-reaction: Arg63, Arg116, Arg7, and Tyr108 required for the relative orientation of the substrate at the active site, the structural rearrangement in the Glu78-Arg90-substrate controls the strength of the hydrogen bonds. The hydrogen bonds connecting the Glu78-Arg90-substrate cooperatively control the stability of TS relative to the ES complex and the positive charge on Arg90 polarizes the substrate in the TS region to gain more electrostatic stabilization. Method: electron quantum chemical calculations by fragment molecular orbital (FMO) method. The structural refinement and reaction path search are performed by the ab initio QM/MM treatment. Usage of the AMBER standard parameter set (parm.96) for the MM force-field calculations. Reaction path search: On the basis of the gas-phase IRC (intrinsic reaction coordinate) profile of chorismate isomerization, the linear reaction path is calculated first
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
rearrangement
The CM reaction is a Claisen rearrangement and is one of the few examples of a biochemical sigmatropic rearrangements
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
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
first committed step in the biosynthesis of the aromatic amino acids tyrosine and phenylalanine in bacteria, fungi and higher plants
-
?
Chorismate
Prephenate
-
shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine
-
?
additional information
?
-
The enzymatic reaction is considered to proceed via a pericyclic transition state
-
-
?
additional information
?
-
-
The enzymatic reaction is considered to proceed via a pericyclic transition state
-
-
?
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
Prephenate
biosynthesis of aromatic amino acids
-
?
Chorismate
Prephenate
first committed step in the biosynthesis of the aromatic amino acids tyrosine and phenylalanine in bacteria, fungi and higher plants
-
?
Chorismate
Prephenate
-
shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chlorogenic acid
CGA, a structural analogue of chorismic acid, is an inhibitor of chorismate mutase, type II regulatory domain (BsCM_2). It binds to BsCM_2 with a higher affinity than chorismate. Similar to BsCM_2, in BsAroH, the chlorogenic acid's position is shifted from the transition state analogue position. The chlorogenic acid interacts with residues Arg63, Val73, Thr74 from one chain and Arg7, Arg90, Val114, Leu115, and Arg116 from the adjacent chain
oxabicyclic dicarboxylic acid
transition state analogon, competitive inhibition
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
-
(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
-
-
chlorogenic acid
CGA, a structural analogue of chorismic acid, is an inhibitor of chorismate mutase, type II regulatory domain (BsCM_2). It binds to BsCM_2 with a higher affinity than chorismate. The BsCM_2-CGA structure has several residues in alternate conformations. His73 exists as alternative conformation in both the chains. At active site S1, the chlorogenic acid makes hydrogen bonds with the side chain of Arg27, Lys38, Gln86, and the main chain atoms of Arg45, Asp47, and Phe79 of chain B. The ligand molecule also interacts with Lys38, Arg50, and Lys80 of chain B, and Arg10 of chain A through water bridge formation. However, at active site S2, along with the above interactions, the ligand forms a direct hydrogen bond with Lys80 and an additional water bridge-mediated hydrogen bond with Gln86 of chain A
additional information
the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins
-
additional information
the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins
-
additional information
-
the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins
-
additional information
the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins
-
additional information
the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins
-
additional information
-
the similarity of chlorogenic acid's interaction with both monofunctional chorismate mutases BsAroH and BsCM_2 may result in similar binding to both proteins
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Most essential residue in BsCM is Arg90, the lack of Arg90 leads to a charge loss of catalytic activity. Two important catalytic roles of Arg90: one is to control the relative stability of the substrate through the collective hydrogen-bonding network in the Glu78-Arg90-substrate, and the other is to polarize the substrate at the appropriate location on the reaction path to gain the maximum electrostatic stabilisation factor for TSS
-
additional information
-
Most essential residue in BsCM is Arg90, the lack of Arg90 leads to a charge loss of catalytic activity. Two important catalytic roles of Arg90: one is to control the relative stability of the substrate through the collective hydrogen-bonding network in the Glu78-Arg90-substrate, and the other is to polarize the substrate at the appropriate location on the reaction path to gain the maximum electrostatic stabilisation factor for TSS
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4
chorismate
-
30°C, pH 7.5, mutant DELTA119-127/D118N, with 5.8 mM substrate
15
chorismate
-
30°C, pH 7.5, mutant DELTA118-127/K111N/A112S/V113N, with 4 mM substrate
16
chorismate
-
30°C, pH 7.5, mutant DELTA118-127/R116L/P117T, with 3.9 mM substrate
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
chorismate
-
30°C, pH 7.5, mutant DELTA119-127/D118N, with 5.8 mM substrate
26
chorismate
-
30°C, pH 7.5, mutant DELTA117-127, with 3.8 mM substrate and DELTA 118-127/R116L/P117T, with 3.9 mM substrate
30
chorismate
-
30°C, pH 7.5, mutant DELTA118-127/K111N/A112S/V113N, with 4 mM substrate
additional information
additional information
R90Cit 10E4-fold decrease in the catalytic activity of kcat. R90K 10E4-fold decrease in the catalytic activity of kcat/Km is obtained
-
additional information
additional information
-
R90Cit 10E4-fold decrease in the catalytic activity of kcat. R90K 10E4-fold decrease in the catalytic activity of kcat/Km is obtained
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00032 - 0.0029
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
0.23
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
30°C, pH 7.5, wild-type
0.001
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
30°C, pH 7.5, wild-type
0.051
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
30°C, pH 7.5, mutant DELTA117-127
0.00032
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
30°C, pH 7.5, wild-type
0.0029
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
30°C, pH 7.5, mutant DELTA117-127
additional information
oxabicyclic dicarboxylic acid
>> 1 mM mutant C88S/R90K
additional information
oxabicyclic dicarboxylic acid
-
>> 1 mM mutant C88S/R90K
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Activation Energies in the enzyme reactions by AMBER and FMO calculations for wild-type and mutants are shown. These results are potential energy, not free energy
additional information
-
Activation Energies in the enzyme reactions by AMBER and FMO calculations for wild-type and mutants are shown. These results are potential energy, not free energy
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
There are four published structures of the Bacillus subtilis wild-type chroismate mutase (CM) with Protein Data Bank (PDB) codes 1COM, 2CHS, 2CHT, and 1DBF
swissprot
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the N-terminal domain of DAHPS from Bacillus subtilis is homologous to the AroQ class of chorismate mutase, type II. Bacillus subtilis also contains a monofunctional AroH class of chorismate mutase situated downstream of the shikimate pathway
malfunction
mutant Arg90Cit, a sluggish variant of Bacillus subtilis chorismate mutase, in which a cationic active-site arginine is replaced by a neutral citrulline, is a poor catalyst even though it effectively preorganizes chorismate for the reaction
physiological function
evolution
the N-terminal domain of DAHPS from Bacillus subtilis is homologous to the AroQ class of chorismate mutase, type II. Bacillus subtilis also contains a monofunctional AroH class of chorismate mutase situated downstream of the shikimate pathway
physiological function
in Bacillus subtilis, the N-terminal domain of the bifunctional 3-deoxy-D-arabino-heptulosonate-7-phosphate-synthase (DAHPS), the first enzyme of the shikimate pathway, belongs to an AroQ class of chorismate mutase and is functionally homologous to the downstream AroH class chorismate mutase. BsCM_2 has a regulatory function in the bifunctional DAHPS enzyme, regulation of DAHPS enzyme activity by the CM2 domain, overview
additional information
physiological function
in Bacillus subtilis, the N-terminal domain of the bifunctional 3-deoxy-D-arabino-heptulosonate-7-phosphate-synthase (DAHPS), the first enzyme of the shikimate pathway, belongs to an AroQ class of chorismate mutase and is functionally homologous to the downstream AroH class chorismate mutase. BsCM_2 may also have a regulatory function in the bifunctional DAHPS enzyme
physiological function
the enzyme catalyzes the rearrangement of chorismate to prephenate. Calculations have predicted the decisive factor in chorismate mutase catalysis to be ground state destabilization rather than transition state stabilization
additional information
AroH molecular docking, using crystal structure of BsAroH, PDB ID 2CHT, overview
additional information
AroH molecular docking, using crystal structure of BsAroH, PDB ID 2CHT, overview
additional information
-
AroH molecular docking, using crystal structure of BsAroH, PDB ID 2CHT, overview
additional information
structural basis of ligand binding into the active site of AroQ class of chorismate mutase from crystal structure analysis, conformational flexibility of active site loop, overview. Molecular dynamics results show that helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. BsCM_2 active site architecture and its regulatory role, molecular dynamics simulation, overview
additional information
structural basis of ligand binding into the active site of AroQ class of chorismate mutase from crystal structure analysis, conformational flexibility of active site loop, overview. Molecular dynamics results show that helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. BsCM_2 active site architecture and its regulatory role, molecular dynamics simulation, overview
additional information
-
structural basis of ligand binding into the active site of AroQ class of chorismate mutase from crystal structure analysis, conformational flexibility of active site loop, overview. Molecular dynamics results show that helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. BsCM_2 active site architecture and its regulatory role, molecular dynamics simulation, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
-
chorismate mutase/prephenate dehydratase, enzyme form CM2, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
in the BsCM_2-chlorogenic acid structure, two active sites, S1 and S2, are located at the interface of two monomers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of double mutants C88S/R90K and C88K/R90S, hanging drop vapour diffusion method at room temperature, space group R3 with a and b: 82.6 A and c: 42.8 A
hanging drop vapor-diffusion method at room temperature and high ionic strength, orthorhombic space group P212121 with a: 52.2 A, b: 83.8 A, c: 86.0 A, nine sulfate ions, five glycerol molecules, 424 water molecules
Performance of molecular dynamics simulations for the three enzyme-ligand complexes(CHOR,PRE and TSA) in addition to the TPS calculations. 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid as a TSA. The principal component analysis (PCA) to analyze structures is used
purified recombinant wild-type enzyme, hanging drop vapor diffusion technique, mixing of 0.001 ml of 3 mM protein in 10 mM Tris buffer, pH 7.5, 2 mM DTT, and 0.125 mM EDTA with 0.001 ml of reservoir solution containing 100 mM malic acid, Mes, Tris (MMT buffer) (in molar ratios of 1:2:2, respectively), pH 6.0, 100-150 mM MgCl2, 25% w/v PEG 1000, and 0.3 mM NaN3, at 20°C, 4-5 days, X-ray diffraction structure determination and analysis at resolution at 1.59 A resolution, molecular replacement using crystal structure PDB ID 1DBF as search model. Purified recombinant mutant enzyme Arg90Cit free or complexed with either substrate, product, or a transition state analogue, hanging drop vapor diffusion technique, mixing of 750 nl of 3 mM protein in 20 mM Tris, pH 8.0, 0.6 mM PMSF, 0.3 mM NaN3 with 750 nl of reservoir solution 100 mM MMT buffer pH 6.0, 50-150 mM CaCl2, 24-26% w/v PEG 1000, and 0.3 mM NaN3, at 20°C, 3-4 days, X-ray diffraction structure determination and analysis at resolution at 1.61-1.80 A resolution, modeling
purified recombinant enzyme AroQ (BsCM_2) in complex with citrate and chlorogenic acid, sitting drop vapor diffusion method, mixing of 0.001 ml of 18 mg/ml protein in 25 mM Tris-HCl, pH 7.5, and 50 mM NaCl, with 0.001 ml of reservoir solution containing 1 M ammonium sulphate, 0.1 M potassium sodium tartrate, and 0.1 M sodium citrate, pH 5.8, 20°C, 15 days, X-ray diffraction structure determination and analysis at 1.9 A and 1.8 A resolution, respectively, molecular replacement using the structure of the N-terminal CM domain of bifunctional DAHPS from Listeria monocytogens (PDB ID 3NVT) as template
structure of N-terminal domain AroQ in complex with citrate and chlorogenic acid at 1.9 A and 1.8 A resolution, respectively. Helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. Chlorogenic acid binds with a higher affinity than chorismate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R90K
The ES, TS, and product structures of the mutants are determined based on the wild-type structure. The hydrogen-bond lengths of the mutants differ from the wild-type. The two mutants chemical reaction progresses in a similar way. No large geometrical changes in and around the active site along the reaction path: only a small rearrangement of the hydrogen-bond sites. As for Lys90/Cit90 mutant reactions, no large conformational change is observed in the overall protein structure except for the geometries around the mutation point. Although the catalytic activity of R90K is inferior to that of the wild-type, the enzymatic mechanism of the R90K mutant is similar to the wild-type. The main anticatalytic factor of R90Cit mutant is the ES stabilization as a result of destabilizing the substrate by the surrounding electrostatic field because of the mutated enzyme. Therefore the TS stabilization mechanism of the Cit90 mutant is quite different from that of the wild-type BsCM
DELTA117-127
DELTA118-127
-
large increase in KM and slower turnover relative to wild-type enzyme
DELTA118-127/K111N/A112S/V113N
-
large increase in KM and slower turnover relative to wild-type enzyme
DELTA118-127/R116L/P117T
-
large increase in KM and slower turnover relative to wild-type enzyme
DELTA119-127/D118N
-
large increase in KM and slower turnover relative to wild-type enzyme
additional information
DELTA117-127
-
large increase in KM and slower turnover relative to wild-type enzyme
additional information
mutant Arg90Cit, a sluggish variant of Bacillus subtilis chorismate mutase, in which a cationic active-site arginine is replaced by a neutral citrulline, is a poor catalyst even though it effectively preorganizes chorismate for the reaction
additional information
-
mutant Arg90Cit, a sluggish variant of Bacillus subtilis chorismate mutase, in which a cationic active-site arginine is replaced by a neutral citrulline, is a poor catalyst even though it effectively preorganizes chorismate for the reaction
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of enzyme BsCM in Escherichia coli strain KA13
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lorence, J.H.; Nester, E.W.
Multiple molecular forms of chorismate mutase in Bacillus subtilis
Biochemistry
6
1541-1553
1967
Bacillus subtilis, Bacillus subtilis 23
Gray, J.V.; Golinelli-Pimpaneau, B.; Knowles, J.R.
Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli
Biochemistry
29
376-383
1990
Bacillus subtilis
Ladner, J.E.; Reddy, P.; Davis, A.; Tordova, M.; Howard, A.J.; Gilliland, G.L.
The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer
Acta Crystallogr. Sect. D
56
673-683
2000
Bacillus subtilis (P19080)
-
Gamper, M.; Hilvert, D.; Kast, P.
Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random protein-termination strategy
Biochemistry
39
14087-14094
2000
Bacillus subtilis
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
Marti, S.; Andres, J.; Moliner, V.; Silla, E.; Tunon, I.; Bertran, J.
A comparative study of claisen and cope rearrangements catalyzed by chorismate mutase. An insight into enzymatic efficiency: transition state stabilization or substrate preorganization?
J. Am. Chem. Soc.
126
311-319
2004
Bacillus subtilis
Kast, P.; Grisostomi, C.; Chen, I.A.; Li, S.; Krengel, U.; Xue, Y.; Hilvert, D.
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
J. Biol. Chem.
275
36832-36838
2000
Bacillus subtilis (P19080), Bacillus subtilis
Ranaghan, K.E.; Mulholland, A.J.
Conformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase
Chem. Commun. (Camb.)
2004
1238-1239
2004
Bacillus subtilis
-
Szefczyk, B.; Mulholland, A.J.; Ranaghan, K.E.; Sokalski, W.A.
Differential transition-state stabilization in enzyme catalysis: quantum chemical analysis of interactions in the chorismate mutase reaction and prediction of the optimal catalytic field
J. Am. Chem. Soc.
126
16148-16159
2004
Bacillus subtilis
Marti, S.; Moliner, V.; Tunon, I.; Williams, I.H.
Computing kinetic isotope effects for chorismate mutase with high accuracy. A new DFT/MM strategy
J. Phys. Chem. B
109
3707-3710
2005
Bacillus subtilis
Ishida, T.; Fedorov, D.G.; Kitaura, K.
All electron quantum chemical calculation of the entire enzyme system confirms a collective catalytic device in the chorismate mutase reaction
J. Phys. Chem. B
110
1457-1463
2006
Bacillus subtilis (P19080), Bacillus subtilis
Crehuet, R.; Field, M.J.
A transition path sampling study of the reaction catalyzed by the enzyme chorismate mutase
J. Phys. Chem. B
111
5708-5718
2007
Bacillus subtilis (P19080)
Ishida, T.
Effects of point mutation on enzymatic activity: Correlation between protein electronic structure and motion in chorismate mutase reaction
J. Am. Chem. Soc.
132
7104-7118
2010
Bacillus subtilis (P19080)
Claeyssens, F.; Ranaghan, K.E.; Lawan, N.; Macrae, S.J.; Manby, F.R.; Harvey, J.N.; Mulholland, A.J.
Analysis of chorismate mutase catalysis by QM/MM modelling of enzyme-catalysed and uncatalysed reactions
Org. Biomol. Chem.
9
1578-1590
2011
Bacillus subtilis
Burschowsky, D.; van Eerde, A.; Oekvist, M.; Kienhoefer, A.; Kast, P.; Hilvert, D.; Krengel, U.
Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis
Proc. Natl. Acad. Sci. USA
111
17516-17521
2014
Bacillus subtilis (P19080), Bacillus subtilis
Pratap, S.; Dev, A.; Kumar, V.; Yadav, R.; Narwal, M.; Tomar, S.; Kumar, P.
Structure of chorismate mutase-like domain of DAHPS from Bacillus subtilis complexed with novel inhibitor reveals conformational plasticity of active site
Sci. Rep.
7
6364
2017
Bacillus subtilis (P19080), Bacillus subtilis (P39912), Bacillus subtilis, Bacillus subtilis 168 (P19080), Bacillus subtilis 168 (P39912)
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