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Information on EC 5.4.99.5 - chorismate mutase
for references in articles please use BRENDA:EC5.4.99.5
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EC Tree 5 Isomerases
5.4 Intramolecular transferases
5.4.99 Transferring other groups
5.4.99.5 chorismate mutase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 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
showSynonyms
chorismate mutase, p-protein, chorismate mutase/prephenate dehydratase, chorismate mutase-prephenate dehydrogenase, bacillus subtilis chorismate mutase, cm type 2, atcm1, rv1885c, cm0819, chorismate mutase 1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
105-MtCM
90-MtCM
aro7
AroA
AroH
AroQ
Bphy_7813
BsAroH
BsCM
BsCM_2
BTH_I1596
chorismate mutase
chorismate mutase-prephenate dehydratase
-
bifunctional enzyme, cf. 4.2.1.51
chorismate mutase-prephenate dehydrogenase
Chorismate mutase/prephenate dehydratase
CM
CM type 2
CM-prephenate dehydratase
CM-TyrAp
CM/PDT/PDHG
trifunctional enzyme EC 5.4.99.5 (chorismate mutase)/EC 4.2.1.51 (prephenate dehydratase)/EC 1.3.1.12 (prephenate dehydrogenase)
CM1
CM2
EcCM
MjCM
MTB CM
MtbCM
MtCM
Mutase, chorismate
-
-
-
-
Mycobacterium tuberculosis H37Rv chorismate mutase
P protein
-
-
-
-
PheA
Rv0948c
Rv1885c
Tparo7
TtCM
AroQ
gene name. Trifunctional enzyme EC 5.4.99.5 (chorismate mutase)/EC 4.2.1.51 (prephenate dehydratase)/EC 1.3.1.12 (prephenate dehydrogenase)
chorismate mutase
belongs to the *AroQclass of chorismate mutases
chorismate mutase
belongs to the *AroQclass of chorismate mutases
-
Chorismate mutase/prephenate dehydratase
-
-
-
-
Chorismate mutase/prephenate dehydratase
-
bifunctional enzyme, cf. EC 4.2.1.51
Chorismate mutase/prephenate dehydratase
Paracidovorax citrulli KACC17005
-
bifunctional enzyme, cf. EC 4.2.1.51
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Chorismate = prephenate
-
-
-
-
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
CMs are extremly versatile enzymes and can be structurally divided into two major groups: the type I or AroH class, which comprises CMs characterized by a trimericpseudo alpha/beta-barrel structure, and the type II or AroQ class, which comprises CMs can also be monofunctional, bifunctional (generally fused to another shikimate pathway member), exported, and/or allosterically regulated
Chorismate = prephenate
Three active sites are formed in the interstices between three subunits. Each active site is composed of the residues of two adjacent subunits. The two Arg hold the chorismate. Crucial distance between Arg6 and Arg63* controls the conformation of the chorismate. The residues in the close vicinity to the chorismate substrate are Arg6, Glu77, Arg89, Tyr 107, Leu114, and Arg115 from one subunit and Phe57*, Ala59*, Arg63*, Leu72*, and Leu73* from the other subunit. The family of the chorismate mutase enzymes shares a common E.S active site
-
Chorismate = prephenate
the active site is formed within a single chain without any contribution from the second chain in a dimer
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
Chorismate = prephenate
CMs are extremly versatile enzymes and can be strucurally divided into two major groups: the type I or AroH class, which comprises CMs characterized by a trimericpseudo alpha/beta-barrel structure, and the type II or AroQ class, which comprises CMs, can also be monofunctional, bifunctional (generally fused to another shikimate pathway member), exported, and/or allosterically regulated
-
-
Chorismate = prephenate
via near attack conformation and transition state intermediates, reaction mechanism, overview
-
Chorismate = prephenate
the enzyme catalyzes the conversion of chorismate to prephenate, which is formally a Claisen rearrangement that proceeds via an endo-oxabicyclic transition state with a chair-like geometry
Chorismate = prephenate
catalytic reaction mechanism, role of conformational dynamics and entropies in enzyme catalysis, overview. Large-scale conformational dynamics make important catalytic contributions to sampling conformational regions in favor of binding the transition state of substrate
Chorismate = prephenate
the active site is formed within a single chain without any contribution from the second chain in a dimer
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular
-
isomerization
pericyclic Claisen rearrangement
rearrangement
isomerization
-
-
-
-
rearrangement
The CM reaction is a Claisen rearrangement and is one of the few examples of a biochemical sigmatropic rearrangements
rearrangement
example of an enzyme-catalyzed pericyclic process known as Claisen rearrangement
rearrangement
-
-
example of an enzyme-catalyzed pericyclic process known as Claisen rearrangement
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
bacilysin biosynthesis, L-phenylalanine biosynthesis I, L-phenylalanine biosynthesis II, L-tyrosine biosynthesis I, L-tyrosine biosynthesis II, L-tyrosine biosynthesis III, salinosporamide A biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
Chorismate pyruvatemutase
-
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CAS REGISTRY NUMBER
COMMENTARY
9068-30-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Chorismate
?
-
Substrates: catalyzes the first step in the branch of the shikimate pathway which leads to the aromatic amino acids, Phe and Tyr
Products: -
Products: -
?
Chorismate
?
-
Substrates: 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
Products: -
Products: -
?
Chorismate
?
-
Substrates: plastidic isoenzyme is elicitor-inducible and pathogen-inducible
Products: -
Products: -
?
Chorismate
?
-
Substrates: in the biosynthesis of Phe and Tyr, there are two enzymes or enzyme complexes metabolizing chorismate, one leading through prephenate to phenylpyruvate and the other leading through prephenate to 4-hydroxyphenylpyruvate
Products: -
Products: -
?
Chorismate
?
-
Substrates: in the biosynthesis of Phe and Tyr, there are two enzymes or enzyme complexes metabolizing chorismate, one leading through prephenate to phenylpyruvate and the other leading through prephenate to 4-hydroxyphenylpyruvate
Products: -
Products: -
?
Chorismate
?
-
Substrates: the first enzyme of the terminal biosynthetic pathway of Phe and Tyr
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: the enzyme is involved in aromatic amino acid biosynthesis
Products: -
Products: -
?
Chorismate
Prephenate
Q9Y7B2
Substrates: enzyme of the first branch point of aromatic amino acid biosynthesis
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: first committed step in the biosynthesis of the aromatic amino acids tyrosine and phenylalanine in bacteria, fungi and higher plants
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine
Products: -
Products: -
?
Chorismate
Prephenate
Burkholderia thailandensis ATCC 700388 / DSM 13276 / CIP 106301 / E264
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: (-)-chorismate. No activity with (+)-chorismate
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: reversible only in presence of P-protein
Products: -
Products: -
r
Chorismate
Prephenate
-
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: phenylalanine biosynthesis
Products: -
Products: -
r
Chorismate
Prephenate
-
Substrates: shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: (-)-chorismate. No activity with (+)-chorismate
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: (-)-chorismate. No activity with (+)-chorismate
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: the enzyme catalyzes the Claisen rearrangement of chorismate to prephenate
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: the rearrangement of chorismate to prephenate is strongly exergonic and essentially irreversible in nature
Products: -
Products: -
ir
Chorismate
Prephenate
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: -
Products: -
Products: -
r
Chorismate
Prephenate
Substrates: -
Products: -
Products: -
r
Chorismate
Prephenate
Mycobacterium tuberculosis ATCC 25618 / H37Rv
Substrates: the rearrangement of chorismate to prephenate is strongly exergonic and essentially irreversible in nature
Products: -
Products: -
ir
Chorismate
Prephenate
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: the enzyme catalyzes the Claisen rearrangement of chorismate to prephenate
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: the bifunctional enzyme (cf. EC 4.2.1.51) possesses two distinct domains: chorismate mutase and prephenate dehydratase
Products: -
Products: -
r
Chorismate
Prephenate
Paracidovorax citrulli KACC17005
-
Substrates: the bifunctional enzyme (cf. EC 4.2.1.51) possesses two distinct domains: chorismate mutase and prephenate dehydratase
Products: -
Products: -
r
Chorismate
Prephenate
Substrates: interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: the PchB-catalyzed reaction is entropy-driven. The entropic effect of the substrate preorganization step is calculated. The entropic effect in the PchB-catalyzed chorismate mutase reaction is determined computationally using a comprehensive multiscale QM/MM MD investigation
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: enzyme of the first branch point of aromatic amino acid biosynthesis
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
additional information
?
-
Substrates: The enzymatic reaction is considered to proceed via a pericyclic transition state
Products: -
Products: -
?
additional information
?
-
-
Substrates: The enzymatic reaction is considered to proceed via a pericyclic transition state
Products: -
Products: -
?
additional information
?
-
Substrates: the isozyme encoded by Rv1885c is characterized as a mono-functional chorismate mutase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the isozyme encoded by Rv1885c is characterized as a mono-functional chorismate mutase
Products: -
Products: -
?
additional information
?
-
Mycobacterium tuberculosis ATCC 25618 / H37Rv
Substrates: the isozyme encoded by Rv1885c is characterized as a mono-functional chorismate mutase
Products: -
Products: -
?
additional information
?
-
Substrates: It is possible that an extracellular biosynthetic pathway from chorismate to phenylalanine exists in Mycobacterium smegmatis, even if the function of such putative route is presently obscure
Products: -
Products: -
?
additional information
?
-
-
Substrates: It is possible that an extracellular biosynthetic pathway from chorismate to phenylalanine exists in Mycobacterium smegmatis, even if the function of such putative route is presently obscure
Products: -
Products: -
?
additional information
?
-
-
Substrates: isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform the chorismate mutase reaction
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform the chorismate mutase reaction
Products: -
Products: -
?
Chorismate
?
-
Substrates: catalyzes the first step in the branch of the shikimate pathway which leads to the aromatic amino acids, Phe and Tyr
Products: -
Products: -
?
Chorismate
?
-
Substrates: 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
Products: -
Products: -
?
Chorismate
?
-
Substrates: plastidic isoenzyme is elicitor-inducible and pathogen-inducible
Products: -
Products: -
?
Chorismate
?
-
Substrates: in the biosynthesis of Phe and Tyr, there are two enzymes or enzyme complexes metabolizing chorismate, one leading through prephenate to phenylpyruvate and the other leading through prephenate to 4-hydroxyphenylpyruvate
Products: -
Products: -
?
Chorismate
?
-
Substrates: in the biosynthesis of Phe and Tyr, there are two enzymes or enzyme complexes metabolizing chorismate, one leading through prephenate to phenylpyruvate and the other leading through prephenate to 4-hydroxyphenylpyruvate
Products: -
Products: -
?
Chorismate
?
-
Substrates: the first enzyme of the terminal biosynthetic pathway of Phe and Tyr
Products: -
Products: -
?
Chorismate
Prephenate
Q9Y7B2
Substrates: enzyme of the first branch point of aromatic amino acid biosynthesis
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: first committed step in the biosynthesis of the aromatic amino acids tyrosine and phenylalanine in bacteria, fungi and higher plants
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine
Products: -
Products: -
?
Chorismate
Prephenate
Burkholderia thailandensis ATCC 700388 / DSM 13276 / CIP 106301 / E264
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: phenylalanine biosynthesis
Products: -
Products: -
r
Chorismate
Prephenate
-
Substrates: shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815
Substrates: -
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
Chorismate
Prephenate
-
Substrates: enzyme of the first branch point of aromatic amino acid biosynthesis
Products: -
Products: -
?
Chorismate
Prephenate
Substrates: biosynthesis of aromatic amino acids
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Mg2+ at concentrations of 0.1-2 mM does not affect CM0819 activity
additional information
-
chorismate mutase activity is only detected when the Mg2+ is not present in the wild-type active site
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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,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,8R)-8-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
(1R,3R,5S,8R)-8-hydroxy-5-nitro-2-azabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
(1R,3R,5S,8R)-8-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
(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,8R)-8-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
(1R,3S,5S,8R)-8-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
(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
(1R,3S,6S,8S,10S)-10-hydroxy-4-oxo-5-oxa-2-azatricyclo[4.3.1.13,8]undecane-8-carboxylic acid
-
(1R,5R,8R)-8-hydroxy-2-oxabicyclo[3.3.1]nona-3,6-diene-3,5-dicarboxylic acid
-
(1R,5S,8R)-8-hydroxy-2-azabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
(1S,2aR,2bR,3S)-4-oxohexahydro-1H-5-oxa-2b-aza-1,3-methanocyclopropa[cd]indene-1-carboxylic acid
-
(1S,3S,5R,6R)-6-hydroxy-4-oxabicyclo[3.3.1]non-7-ene-1,3-dicarboxylate
endo-oxabicyclic dicarboxylic acid is a good geometric mimic of transition state
(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
(2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid
-
(2Z)-2-(4-chlorophenyl)-3-[4-(dimethoxymethyl)-2-nitrophenyl]prop-2-enoic acid
competitive
(3R,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
(3S,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
(3S,6Z)-8-hydroxy-2-oxabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
(Z)-N-(1-acetyl-2-oxoindolin-3-ylidene)hydrazinecarbothioamide
-
-
1-(2-(tert-butyl)-5-chloro-7-(methylsulfonyl)-1H-indol-3-yl)ethan-1-one
45% inhibition at 0.03 mM
1-Substituted adamantane derivatives
-
order of decreasing inhibitory activity with the various substituents: -PO32-, -P(OCH3)O2, CO2-, -CH2CO2-, -SO2-,Y -SO3-
1-[[1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 67.67% inhibition
1-[[1-(benzenesulfonyl)-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 74.2% inhibition
1-[[1-(benzenesulfonyl)-1H-indol-2-yl]methyl]-3-hydroxy-1,3-dihydro-2H-indol-2-one
0.03 mM, 10.26% inhibition
1-[[1-(benzenesulfonyl)-5,7-dimethyl-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 67.30% inhibition
1-[[1-(methanesulfonyl)-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 70.28% inhibition
1-[[1-(methanesulfonyl)-5,7-dimethyl-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 72.92% inhibition
1-[[1-(thiophene-2-sulfonyl)-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 47.93% inhibition
1-[[5,7-dimethyl-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 71.61% inhibition
1-[[5-bromo-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 67.53% inhibition
1-[[5-chloro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 66,83% inhibition
1-[[5-chloro-1-(methanesulfonyl)-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 73.43% inhibition
1-[[5-fluoro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1H-indole-2,3-dione
0.03 mM, 71.36% inhibition
2-chloro-4-(ethoxycarbonyl)-1-hydroxy-6-methylquinolin-1-ium
-
2-[2-[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]ethyl]-4-methylpentanoic acid
competitive
3-((dihydroxyamino)thio)-4-((3,5-dimethoxyphenethyl)amino)-5-nitrobenzoic acid
competitive
3-endo,8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
potent
3-hydroxy-1-[[1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1,3-dihydro-2H-indol-2-one
0.03 mM, 18.65% inhibition
3-hydroxy-1-[[1-(methanesulfonyl)-1H-indol-2-yl]methyl]-1,3-dihydro-2H-indol-2-one
0.03 mM, 5.93% inhibition
3-[[1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 56% inhibition
3-[[1-(benzenesulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 42% inhibition
3-[[1-(benzenesulfonyl)-1H-indol-2-yl]methyl]-5-methyl-7-propyl-3,5-dihydro-4H-pyrazolo[4,3-d][1,2,3]triazin-4-one
0.03 mM, 25% inhibition
3-[[1-(benzenesulfonyl)-5,7-dimethyl-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 27% inhibition
3-[[1-(methanesulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 20% inhibition
3-[[1-(methanesulfonyl)-1H-indol-2-yl]methyl]-5-methyl-7-propyl-3,5-dihydro-4H-pyrazolo[4,3-d][1,2,3]triazin-4-one
0.03 mM, 37% inhibition
3-[[1-(methanesulfonyl)-5,7-dimethyl-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 37% inhibition
3-[[1-(methanesulfonyl)-5-nitro-1H-indol-2-yl]methyl]-5-methyl-7-propyl-3,5-dihydro-4H-pyrazolo[4,3-d][1,2,3]triazin-4-one
0.03 mM, 30% inhibition
3-[[1-(thiophene-2-sulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 45% inhibition
3-[[5-bromo-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 38% inhibition
3-[[5-chloro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 78% inhibition
3-[[5-chloro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-5-methyl-7-propyl-3,5-dihydro-4H-pyrazolo[4,3-d][1,2,3]triazin-4-one
0.03 mM, 70% inhibition
3-[[5-chloro-1-(methanesulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 26% inhibition
3-[[5-chloro-1-(methanesulfonyl)-1H-indol-2-yl]methyl]-5-methyl-7-propyl-3,5-dihydro-4H-pyrazolo[4,3-d][1,2,3]triazin-4-one
0.03 mM, 5% inhibition
3-[[5-chloro-1-(thiophene-2-sulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 57% inhibition
3-[[5-fluoro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 41% inhibition
3-[[5-fluoro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-5-methyl-7-propyl-3,5-dihydro-4H-pyrazolo[4,3-d][1,2,3]triazin-4-one
0.03 mM, 7% inhibition
3-[[5-fluoro-1-(methanesulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 29% inhibition
5-methyl-3-[[1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-7-propyl-3,5-dihydro-4H-pyrazolo[4,3-d][1,2,3]triazin-4-one
0.03 mM, 20% inhibition
5-methyl-3-[[5-methyl-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-7-propyl-3,5-dihydro-4H-pyrazolo[4,3-d][1,2,3]triazin-4-one
0.03 mM, 19% inhibition
5-naphthyl-7-propyl-3H-pyrazolo[4,3-d][1,2,3]triazin-4(5H)-one
-
6'-iodo-1,3-dihydro-1'H-spiro[indene-2,2'-quinazolin]-4'(3'H)-one
a spiro 2,3-dihydroquinazolin-4(1H)-one
6-bromo-3-[[5-chloro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
0.03 mM, 34% inhibition
8-exo-8-Hydroxy-2-oxabicyclo[3.3.1]nona-3,6-diene-3,5-dicarboxylic acid
-
slight
8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
competitive inhibition
adamantane-1-phosphonate
-
no inhibitory effect up to concentrations of 0.1 and 1 mM
ethyl 2-([[1-(benzenesulfonyl)-1H-indol-2-yl]methyl]amino)benzoate
0.03 mM, 15.34% inhibition
ethyl 2-([[1-(methanesulfonyl)-1H-indol-2-yl]methyl]amino)benzoate
0.03 mM, 26.29% inhibition
ethyl 2-([[5-bromo-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]amino)benzoate
0.03 mM, 9.59% inhibition
ethyl 2-([[5-chloro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]amino)benzoate
0.03 mM, 4.54% inhibition
ethyl 2-([[5-chloro-1-(methanesulfonyl)-1H-indol-2-yl]methyl]amino)benzoate
0.03 mM, 14.18% inhibition
ethyl 2-([[5-fluoro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]amino)benzoate
0.03 mM, 1.38% inhibition
ethyl 4-(2-(4-hydroxybut-1-yn-1-yl)phenyl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
methyl 2-([[5-chloro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]amino)benzoate
0.03 mM, 14.12% inhibition
N-(4-fluoro-2-(5-fluoro-1-(methylsulfonyl)-1H-inden-2-yl)phenyl)methanesulfonamide
-
N-[(3-(2-amino-3-cyano-2H-benzo[h]chromen-4-y))phenyl]methylidyne]-2-hydroxyethanaminium
-
N-[[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]carbonyl]leucine
-
NaCl
-
inhibition is cooperative, NaCl also increases the sensitivity of the enzyme to inhibition by Phe
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
-
-
(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,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,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
-
3-(3-methoxyphenyl)-5,6,7,8-tetrahydrobenzo[b]thieno[2,3d]pyrimidin-4[3H]-one
-
3-(3-methoxyphenyl)-5,6,7,8-tetrahydrobenzo[b]thieno[2,3d]pyrimidin-4[3H]-one
-
-
3-amino-1-(3-(4-hydroxybut-1-yn-1-yl)phenyl)-1H-benzol[f]chromene-2-carbonitril
-
3-amino-1-(3-(4-hydroxybut-1-yn-1-yl)phenyl)-1H-benzol[f]chromene-2-carbonitril
-
-
4-(3,4-dimethoxyphenethylamino)-3-nitro-5-sulfamoylbenzoic acid
-
-
4-(3,4-dimethoxyphenethylamino)-3-nitro-5-sulfamoylbenzoic acid
-
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid
-
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid
0.03 mM, 56.97% inhibition
5-naphthyl-7-propyl-3H-pyrazolo-[4,3-d][1,2,3]triazin-4[5h]-one
-
5-naphthyl-7-propyl-3H-pyrazolo-[4,3-d][1,2,3]triazin-4[5h]-one
-
-
caffeic acid
-
enzyme forms CM1 and CM2 are inhibited, enzyme form CM3 is unaffected
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; 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
chlorogenic acid
-
enzyme forms CM1 and CM2 are inhibited, enzyme form CM3 is unaffected
L-Phe
-
chorismate mutase P is strongly inhibited, chorismate mutase T is not inhibited
L-Phe
Penicillium duponti
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited; enzyme form CM3 is inhibited
L-tryptophan
-
allosteric. The Trp at the dimer interface interacts extensively with residues from both subunits. The unexpected gene duplication possibly leads to a different allosteric regulation mechanism than that is known for other CMs
L-Tyr
-
slight inhibition of chorismate mutase P and no inhibition of chorismate mutase T
L-Tyr
Penicillium duponti
-
enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited; enzyme form CM3 is inhibited
L-Tyr
-
Trp reverses inhibition; enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited
L-Tyr
-
wild-type enzyme is inhibited. Mutant enzymes with amino acid exchange at Thr234, especially Tyr234Phe, mutant enzyme Ile225Thr and Ile225Thr/Thr226Ile are insensitive
phenylalanine
model of the AtCM1x02phenylalanine complex including residues Arg79-Val290 and Val307-Asp340, the phenylalanine ligand, and 83 waters, inhibits about 20fold
phenylalanine
-
inhibits chorismate mutase by interenzyme allostery
tyrosine
is a negative effector for the enzyme; is a negative effector for the enzyme
tyrosine
is a negative effector for the enzyme; is a negative effector for the enzyme
tyrosine
negatively regulated by tryptophan. The enzyme binds tyrosine and tryptophan with negative homotrophic cooperativity. It can simultaneously bind tyrosine and tryptophan
tyrosine
allosteric inhibition. Protein dynamics and conformational entropy play important roles in allosteric regulation
tyrosine
-
conformational transitions in yeast chorismate mutase is important for allosteric regulation
tyrosine
competitive inhibition, 0.5 M tyrosine leads to 40% inhibition
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
activity is not affected by both amino acids Phe and Tyr at concentrations up to 0.5 mM
-
additional information
-
activity is not affected by both amino acids Phe and Tyr at concentrations up to 0.5 mM
-
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; 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; 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; 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 enzyme is greatly inhibited at acidic pH. L-phenylalanine, L-tyrosine, and L-tryptophan moderately enhance activity at low concentrations, but they inhibit the enzyme at higher concentrations
-
additional information
-
Unlike the other known prokaryotic CMs, the Mycobacterium tuberculosis enzyme exhibits allosteric regulation by aromatic amino acids, a feature limited to the eukaryotic CMs. The active site of MtbCM is seen to be blocked due to the presence of a sulfate ion in the structure. It therefore appears that sulphate acts as an inhibitor of the enzyme by blocking the entry of the substrate into the active site. In MtbCM the allosteric site is close to the active site
-
additional information
aza inhibitors. Competitive inhibition, Saccharomyces cerevisiae chorismate mutase inhibitors and the substrate chorismic acid used for pharmacophore model generation. These inhibitors do not alter Vmax at the higher concentration of substrate (1-5 mM)
-
additional information
-
aza inhibitors. Competitive inhibition, Saccharomyces cerevisiae chorismate mutase inhibitors and the substrate chorismic acid used for pharmacophore model generation. These inhibitors do not alter Vmax at the higher concentration of substrate (1-5 mM)
-
additional information
*MtCM is not regulated by the aromatic amino acids. The x-ray structure of *MtCM does not have an allosteric regulatory site in the protein
-
additional information
-
*MtCM is not regulated by the aromatic amino acids. The x-ray structure of *MtCM does not have an allosteric regulatory site in the protein
-
additional information
development and synthesis of transition state analogues and small molecule compounds as enzyme inhibitors
-
additional information
-
development and synthesis of transition state analogues and small molecule compounds as enzyme inhibitors
-
additional information
-
discovery and structure optimization of a series of isatin derivatives as Mycobacterium tuberculosis chorismate mutase inhibitors, synthesis of enzyme inhibitors, overview
-
additional information
identification and structure-activity relationship study of carvacrol derivatives as Mycobacterium tuberculosis chorismate mutase inhibitors, structure-based e-pharmacophore modeling, overview. Database screening using the crystal structure of the MTB CM bound transition state intermediate (PDB ID 2FP2) as framework. No inhibition by 3-(6-(benzyloxy)-1H-indol-1-yl)propanoic acid, 5-isopropyl-2-methylphenyl acetate, 4-bromo-5-isopropyl-2-methylphenol, 4-nitro-5-isopropyl-2-methylphenol, 4-isopropyl-2-methoxy-1-methylbenzene, 4-bromo-2-isopropyl-5-methylphenol, 4-nitro-2-isopropyl-5-methylphenol, and 4-chloro-2-isopropyl-5-methylphenol
-
additional information
-
identification and structure-activity relationship study of carvacrol derivatives as Mycobacterium tuberculosis chorismate mutase inhibitors, structure-based e-pharmacophore modeling, overview. Database screening using the crystal structure of the MTB CM bound transition state intermediate (PDB ID 2FP2) as framework. No inhibition by 3-(6-(benzyloxy)-1H-indol-1-yl)propanoic acid, 5-isopropyl-2-methylphenyl acetate, 4-bromo-5-isopropyl-2-methylphenol, 4-nitro-5-isopropyl-2-methylphenol, 4-isopropyl-2-methoxy-1-methylbenzene, 4-bromo-2-isopropyl-5-methylphenol, 4-nitro-2-isopropyl-5-methylphenol, and 4-chloro-2-isopropyl-5-methylphenol
-
additional information
neither tyrosine nor phenylalanine alters the activity of enzyme SmCM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arabinose
expression can be induced by arabinose under the control of the araBAD promoter
3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
the catalytic efficiency of chorismate mutase increases 140fold on addition of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, chorismate mutase forms a complex with 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase and that complex formation both increases the CM activity by more than two orders of magnitude and endows chorismate mutase with regulatory features
-
L-Trp
-
wild-type enzyme, mutant enzyme Ile225Thr/Thr226Ile and enzymes with mutations at Tyr234 are activated. No activation of mutant enzyme Thr226Ile
tryptophan
-
chorismate mutase (CgCM) requires the formation of a complex with DAHP synthase (CgDS) to achieve full activity. Both CgCM and CgDS are feedback regulated by aromatic amino acids binding to CgDS. Binding of tryptophan to CgDS strongly activates CgCM
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
tryptophan
-
conformational transitions in yeast chorismate mutase is important for allosteric regulation
tryptophan
allosteric activation. Protein dynamics and conformational entropy play important roles in allosteric regulation
tryptophan
positively regulated by tryptophan. The enzyme binds tyrosine and tryptophan with negative homotrophic cooperativity. It can simultaneously bind tyrosine and tryptophan
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
-
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
-
additional information
-
the CM0819 activity is not affected by L-Phe, L-Tyr or L-Trp (0.01-10 mM), EDTA at concentrations of 0.1-2 mM does not affect CM0819 activity
-
additional information
neither pH variation between 5.9 and 8.7, nor provision of 0.1 mg/ml bovine serum albumin, 2 mM Ca2+, 10 mM Mg2+, 1 mM EDTA, 1 mM EGTA, 1 mM 1,10-phenanthroline, 1 mM L-phenylalanine, 1 mM L-tyrosine, 1 mM L-tryptophan, or 0.6 mM salicylate affect catalytic activity by more than a factor of 2
-
additional information
-
neither pH variation between 5.9 and 8.7, nor provision of 0.1 mg/ml bovine serum albumin, 2 mM Ca2+, 10 mM Mg2+, 1 mM EDTA, 1 mM EGTA, 1 mM 1,10-phenanthroline, 1 mM L-phenylalanine, 1 mM L-tyrosine, 1 mM L-tryptophan, or 0.6 mM salicylate affect catalytic activity by more than a factor of 2
-
additional information
CM2 is not allosterically regulated by L-tryptophan, L-phenylalanine, or L-tyrosine
-
additional information
CM2 is not allosterically regulated by L-tryptophan, L-phenylalanine, or L-tyrosine
-
additional information
-
CM2 is not allosterically regulated by L-tryptophan, L-phenylalanine, or L-tyrosine
-
additional information
CM1 is allosterically regulated by L-tryptophan but not L-phenylalanine or L-tyrosine
-
additional information
CM1 is allosterically regulated by L-tryptophan but not L-phenylalanine or L-tyrosine
-
additional information
-
CM1 is allosterically regulated by L-tryptophan but not L-phenylalanine or L-tyrosine
-
additional information
neither tyrosine nor phenylalanine alters the activity of enzyme SmCM
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
[CR of All Target Lesions in a Patient with Metastatic Esophageal Cancer and Generalized Weakness Treated with Systemic Chemotherapy after Nutritional Support].
Alzheimer Disease
[Inhibition of neuronal death by promoting degradation of intracellular amyloid beta-protein]
Borna Disease
Borna disease virus P-protein is phosphorylated by protein kinase Cepsilon and casein kinase II.
Communicable Diseases
Crystal structure of chorismate mutase from Burkholderia thailandensis.
Cysts
A chorismate mutase from the soybean cyst nematode Heterodera glycines shows polymorphisms that correlate with virulence.
Cysts
Alternative splicing: A novel mechanism of regulation identified in the chorismate mutase gene of the potato cyst nematode Globodera rostochiensis.
Cysts
Characterization of a chorismate mutase from the potato cyst nematode Globodera pallida.
Cysts
Structural and functional investigation of a secreted chorismate mutase from the plant-parasitic nematode Heterodera schachtii in the context of related enzymes from diverse origins.
Distemper
Comparison of messenger RNAs induced in cells infected with each member of the morbillivirus group.
Distemper
Spot synthesis of overlapping peptides on paper membrane supports enables the identification of linear monoclonal antibody binding determinants on morbillivirus phosphoproteins.
Esophageal Neoplasms
PSMD4 regulates the malignancy of esophageal cancer cells by suppressing endoplasmic reticulum stress.
Glycogen Storage Disease Type II
Specific induction by glycine of the gene for the P-subunit of glycine decarboxylase from Saccharomyces cerevisiae.
Hepatitis B
Expression of the P-protein of the human hepatitis B virus in a vaccinia virus system and detection of the nucleocapsid-associated P-gene product by radiolabelling at newly introduced phosphorylation sites.
Hyperglycinemia, Nonketotic
Enzymatic diagnosis of nonketotic hyperglycinemia with lymphoblasts.
Hyperglycinemia, Nonketotic
Glycine cleavage system: reaction mechanism, physiological significance, and hyperglycinemia.
Hyperglycinemia, Nonketotic
Ketogenic diet in early myoclonic encephalopathy due to non ketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Molecular genetic and potential biochemical characteristics of patients with T-protein deficiency as a cause of glycine encephalopathy (NKH).
Hyperglycinemia, Nonketotic
Nonketotic hyperglycinemia: two patients with primary defects of P-protein and T-protein, respectively, in the glycine cleavage system.
Hyperglycinemia, Nonketotic
Structural and expression analyses of normal and mutant mRNA encoding glycine decarboxylase: three-base deletion in mRNA causes nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Structure of P-protein of the glycine cleavage system: implications for nonketotic hyperglycinemia.
Infections
Antibody response to P-protein in patients with Branhamella catarrhalis infections.
Infections
Nuclear Trafficking of the Rabies Virus Interferon Antagonist P-Protein Is Regulated by an Importin-Binding Nuclear Localization Sequence in the C-Terminal Domain.
Infections
Plant hormones in defense response of Brassica napus to Sclerotinia sclerotiorum - reassessing the role of salicylic acid in the interaction with a necrotroph.
Insulin Resistance
Dehydroepiandrosterone protects against hepatic glycolipid metabolic disorder and insulin resistance induced by high fat via activation of AMPK-PGC-1?-NRF-1 and IRS1-AKT-GLUT2 signaling pathways.
Leiomyoma
Transcervical microwave ablation in type 2 uterine fibroids via a hysteroscopic approach: analysis of ablation profiles.
Lung Neoplasms
Interaction between epidermal growth factor receptor and interleukin-6 receptor in NSCLC progression.
Lung Neoplasms
Sodium Danshensu inhibits the progression of lung cancer by regulating PI3K/Akt signaling pathway.
Lupus Erythematosus, Systemic
Anti-ribosomal P-protein and its role in psychiatric manifestations of systemic lupus erythematosus: myth or reality?
Lymphoma, B-Cell
HIF-?/PKM2 and PI3K-AKT pathways involved in the protection by dexmedetomidine against isoflurane or bupivacaine-induced apoptosis in hippocampal neuronal HT22 cells.
Lymphoma, B-Cell
I157172, a novel inhibitor of cystathionine ?-lyase, inhibits growth and migration of breast cancer cells via SIRT1-mediated deacetylation of STAT3.
Malaria
Plasmodium berghei glycine cleavage system T-protein is non-essential for parasite survival in vertebrate and invertebrate hosts.
Melanoma
Unrevealing the role of P-protein on melanosome biology and structure, using siRNA-mediated down regulation of OCA2.
Neoplasm Metastasis
[A Case of Neuroendocrine Carcinoma Treated with Salvage Surgery after Systemic Chemotherapy].
Neoplasms
Synergistic Activation upon MET and ALK Coamplification Sustains Targeted Therapy in Sarcomatoid Carcinoma, a Deadly Subtype of Lung Cancer.
Neoplasms
[A Case of Neuroendocrine Carcinoma Treated with Salvage Surgery after Systemic Chemotherapy].
Neoplasms
[A case of primary small intestinal cancer accompanied by virchow lymph node metastasis undergoing TS-1 treatment]
Ovarian Neoplasms
Effect of MicroRNA-210 on the Growth of Ovarian Cancer Cells and the Efficacy of Radiotherapy.
Pneumonia
Antibody response to P-protein in patients with Branhamella catarrhalis infections.
Prostatic Neoplasms
Gold-chrysophanol nanoparticles suppress human prostate cancer progression through inactivating AKT expression and inducing apoptosis and ROS generation in vitro and in vivo.
Pulmonary Atelectasis
Arnold-Chiari Malformation and Scoliosis: A Chronic Lung Collapse Mimicking Sepsis.
Rabies
Dual modes of rabies P-protein association with microtubules: a novel strategy to suppress the antiviral response.
Rabies
Interaction of Rabies Virus P-Protein With STAT Proteins is Critical to Lethal Rabies Disease.
Rabies
Nuclear Trafficking of the Rabies Virus Interferon Antagonist P-Protein Is Regulated by an Importin-Binding Nuclear Localization Sequence in the C-Terminal Domain.
Rabies
Nucleocytoplasmic distribution of rabies virus p-protein is regulated by phosphorylation adjacent to C-terminal nuclear import and export signals.
Respiratory Tract Infections
Antibody response to P-protein in patients with Branhamella catarrhalis infections.
Scoliosis
Arnold-Chiari Malformation and Scoliosis: A Chronic Lung Collapse Mimicking Sepsis.
Tuberculosis
1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed.
Tuberculosis
A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis.
Tuberculosis
A novel noncovalent complex of chorismate mutase and DAHP synthase from Mycobacterium tuberculosis: protein purification, crystallization and X-ray diffraction analysis.
Tuberculosis
A Pd-mediated new strategy to functionalized 2-aminochromenes: their in vitro evaluation as potential anti tuberculosis agents.
Tuberculosis
AlCl(3) mediated unexpected migration of sulfonyl groups: regioselective synthesis of 7-sulfonyl indoles of potential pharmacological interest.
Tuberculosis
Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids.
Tuberculosis
Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis.
Tuberculosis
Crystallization and preliminary X-ray crystallographic studies of Mycobacterium tuberculosis chorismate mutase.
Tuberculosis
Diagnostic Potential of IgG and IgA Responses to Mycobacterium tuberculosis Antigens for Discrimination among Active Tuberculosis, Latent Tuberculosis Infection, and Non-Infected Individuals.
Tuberculosis
Discovery and Structure Optimization of a Series of Isatin Derivatives as Mycobacterium tuberculosis Chorismate Mutase Inhibitors.
Tuberculosis
Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance.
Tuberculosis
Functional mapping of protein-protein interactions in an enzyme complex by directed evolution.
Tuberculosis
Identification and structure-activity relationship study of carvacrol derivatives as Mycobacterium tuberculosis chorismate mutase inhibitors.
Tuberculosis
Interaction between DAHP synthase and chorismate mutase endows new regulation on DAHP synthase activity in Corynebacterium glutamicum.
Tuberculosis
Ligand based virtual screening and biological evaluation of inhibitors of chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Molecular dynamics simulation of the last step of a catalytic cycle: Product release from the active site of the enzyme chorismate mutase from Mycobacterium tuberculosis.
Tuberculosis
pheA (Rv3838c) of Mycobacterium tuberculosis encodes an allosterically regulated monofunctional prephenate dehydratase that requires both catalytic and regulatory domains for optimum activity.
Tuberculosis
Preliminary X-ray crystallographic analysis of the secreted chorismate mutase from Mycobacterium tuberculosis: a tricky crystallization problem solved.
Tuberculosis
Purification and characterization of a functionally active Mycobacterium tuberculosis prephenate dehydrogenase.
Tuberculosis
Purified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activity.
Tuberculosis
Remote Control by Inter-Enzyme Allostery: A Novel Paradigm for Regulation of the Shikimate Pathway.
Tuberculosis
Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner.
Tuberculosis
The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions.
Tuberculosis
Understanding the different activities of highly promiscuous MbtI by computational methods.
Tuberculosis
When inhibitors do not inhibit: critical evaluation of rational drug design targeting chorismate mutase from Mycobacterium tuberculosis.
Vaccinia
Expression of the P-protein of the human hepatitis B virus in a vaccinia virus system and detection of the nucleocapsid-associated P-gene product by radiolabelling at newly introduced phosphorylation sites.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.022
chorismate
pH 7.5, 30°C, mutant enzyme V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88D/G89A/H90M
0.03
chorismate
-
mutant enzyme V35A, in PBS buffer (pH 7.5) at 20°C
0.038
chorismate
pH 7.5, 30°C, mutant enzyme V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88L/G89A/H90M
0.045
chorismate
pH 7.5, 30°C, mutant enzyme V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88N/G89A/H90M
0.054
chorismate
-
wild type enzyme, in PBS buffer (pH 7.5) at 20°C
0.059
chorismate
-
mutant enzyme D48G, in PBS buffer (pH 7.5) at 20°C
0.073
chorismate
-
mutant enzyme F77W, in PBS buffer (pH 7.5) at 20°C
0.15
chorismate
-
leaderless MtCM with C-terminal His tag, at 30°C and pH 7.5
0.15
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.29
chorismate
-
genetically engineered monofunctional chorismate mutase that contains only 109 amino acids
0.4
chorismate
-
chorismate, mutant enzyme Thr226Ile, activated by 0.01 mM Trp
0.5 - 1
chorismate
pH 7.5, 30°C, mutant enzyme T52P/V55D/L88D
0.55
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
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
1.1
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
1.2
chorismate
-
mutant enzyme Q88N, in PBS buffer (pH 7.5) at 20°C
1.3
chorismate
-
mutant enzyme R51Q, in PBS buffer (pH 7.5) at 20°C
1.5
chorismate
-
mutant enzyme Ile225Thr/Thr226Ile, activated by 0.01 mM Trp
2.33
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
2.39
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
3.19
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
4
chorismate
-
30°C, pH 7.5, mutant DELTA119-127/D118N, with 5.8 mM substrate
5.19
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
6.79
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
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
Chorismic acid
Competetive inhibition by I IV Structur: increase the Km
additional information
Chorismic acid
-
Competetive inhibition by I IV Structur: increase the Km
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
-
additional information
additional information
sigmoid substrate saturation curve with S0.5: 16.7 mM for chorismate at 37°C and S0.5: 12 mM for chorismate at 37°C in presence of 0.1 mM tyrosine
-
additional information
additional information
-
sigmoid substrate saturation curve with S0.5: 16.7 mM for chorismate at 37°C and S0.5: 12 mM for chorismate at 37°C in presence of 0.1 mM tyrosine
-
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
A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol)
-
additional information
additional information
-
A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol)
-
additional information
additional information
due to instability of chorismate at higher temperature, a Km value is not determined
-
additional information
additional information
-
due to instability of chorismate at higher temperature, a Km value is not determined
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
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
-
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.042
chorismate
-
mutant enzyme Q88N, in PBS buffer (pH 7.5) at 20°C
0.41
chorismate
-
mutant enzyme F77W, in PBS buffer (pH 7.5) at 20°C
0.5
chorismate
-
mutant enzyme V35A, in PBS buffer (pH 7.5) at 20°C
1.3
chorismate
-
mutant enzyme D48G, in PBS buffer (pH 7.5) at 20°C
2.6
chorismate
-
mutant enzyme R51Q, in PBS buffer (pH 7.5) at 20°C
3
chorismate
-
wild type enzyme, in PBS buffer (pH 7.5) at 20°C
6
chorismate
pH 7.5, 30°C, mutant enzyme V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88L/G89A/H90M
7.6
chorismate
pH 7.5, 30°C, mutant enzyme V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88N/G89A/H90M
9.4
chorismate
pH 7.5, 30°C, mutant enzyme V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88D/G89A/H90M
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
15
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
18.8
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
19.5
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
20.7
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
22.8
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
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
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
40.7
chorismate
-
genetically engineered enzyme containg the amino acid residues 1-300
44.3
chorismate
-
genetically engineered enzyme containg the amino acid residues 1-285
56
chorismate
-
leaderless MtCM with C-terminal His tag, at 30°C and pH 7.5
535
chorismate
-
mutant enzyme Ile225Thr/Thr226Ile, activated by 0.01 mM Trp
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
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
-
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
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
-
additional information
additional information
-
CM spezific activity in Escherichia coli extracts: Control (M. Tuberculosis) Sp act (U/mg) 0.889 Cloned extract/control 1 AroQMt (Rv0948c) Sp act (U/mg) 127.38 Cloned extract/control 143.28 *AroQMt (Rv1885c) Sp act (U/mg) 94.23 Cloned extract/control 105.9. CM specific activity in Escherichia coli cells expressing either the AroQMt or the *AroQMt protein is determined to be, repectively, 143- and 106-fold higher than the enzyme activity obtained for Escherichia coli cells carrying the pET-23a(+) expression vector
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.36
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
3.62
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
4.7
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
8.34
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
8.66
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
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
160
chorismate
pH 7.5, 30°C, mutant enzyme V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88L/G89A/H90M
170
chorismate
pH 7.5, 30°C, mutant enzyme V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88N/G89A/H90M
258
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
430
chorismate
pH 7.5, 30°C, mutant enzyme V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88D/G89A/H90M
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00032 - 0.0076
(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
0.01771
(2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid
-
0.0211
(2Z)-2-(4-chlorophenyl)-3-[4-(dimethoxymethyl)-2-nitrophenyl]prop-2-enoic acid
pH 7.0, 37°C
0.0177
2-[2-[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]ethyl]-4-methylpentanoic acid
pH 7.0, 37°C
0.0057
3-((dihydroxyamino)thio)-4-((3,5-dimethoxyphenethyl)amino)-5-nitrobenzoic acid
pH 7.0, 37°C
0.0057
4-(3,4-dimethoxyphenethylamino)-3-nitro-5-sulfamoylbenzoic acid
pH and temperature not specified in the publication
0.0057
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid
4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid shows the most potent inhibition with Ki value of 0.0057 mM against MtCM
0.0037
8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid
-
-
0.0211
N-[[3-(tert-butoxycarbonyl)-2-phenyl-1,3-thiazolidin-4-yl]carbonyl]leucine
-
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
0.0023
(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
0.051
(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
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
additional information
oxabicyclic dicarboxylic acid
>> 1 mM mutant C88S/R90K
additional information
oxabicyclic dicarboxylic acid
-
>> 1 mM mutant C88S/R90K
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
(Z)-3-((5-nitrothiazol-2-yl)imino)indolin-2-one
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.1
(Z)-3-((6-nitrobenzo[d]thiazol-2-yl)imino)indolin-2-one
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.09814
(Z)-3-(hydroxyimino)indolin-2-one
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0305
(Z)-N-(1-acetyl-2-oxoindolin-3-ylidene)hydrazinecarbothioamide
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.025
(Z)-N-(1-acetyl-2-oxoindolin-3-ylidene)hydrazinecarboxamide
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0669
(Z)-N-(2-oxoindolin-3-ylidene)hydrazinecarbothioamide
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0541
(Z)-N-(2-oxoindolin-3-ylidene)hydrazinecarboxamide
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.09656
1-(prop-1-en-2-yl)indoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.00099
1-acetylindoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0227
1-ethylindoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.02158
1-isopropyl-2-methoxy-4-methylbenzene
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.07512
1-isopropylindoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.00196
1-methylindoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0233
1-phenylindoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.041
1-pivaloylindoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0239
2-chloro-4-(ethoxycarbonyl)-1-hydroxy-6-methylquinolin-1-ium
Mycobacterium tuberculosis
pH 7.0, 37°C
0.00408
2-isopropyl-5-methylphenyl acetate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.01363
2-methyl-5-(prop-1-en-2-yl)cyclohexanol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00093
3-((5-nitrothiophen-2-yl)methylene)indolin-2-one
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.00101
3-(4-nitrobenzylidene)indolin-2-one
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.01974
3-chloroquinoxaline
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0214
3-isopropylphenol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.02677
3-methyl-5-(propan-2-yl)phenol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00085
3-[[5-chloro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-1,2,3-benzotriazin-4(3H)-one
Mycobacterium tuberculosis
pH 7.5, 37°C
0.0004
3-[[5-chloro-1-(4-methylbenzene-1-sulfonyl)-1H-indol-2-yl]methyl]-5-methyl-7-propyl-3,5-dihydro-4H-pyrazolo[4,3-d][1,2,3]triazin-4-one
Mycobacterium tuberculosis
pH 7.5, 37°C
0.0957
5-(2,3-dichlorophenyl)indoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0365
5-(2,5-dimethylphenyl)indoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0557
5-(4-(3-(tert-butyl)phenyl)piperazin-1-yl)indoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0256
5-(4-(furan-2-carbonyl)piperazin-1-yl)indoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0319
5-(4-methylpiperazin-1-yl)indoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0399
5-(piperazin-1-yl)indoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0288
5-(piperidin-1-yl)indoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.01513
5-naphthyl-7-propyl-3H-pyrazolo[4,3-d][1,2,3]triazin-4(5H)-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0371
5-phenylindoline-2,3-dione
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.00106
carvacrol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0148
ethyl 4-(2-(4-hydroxybut-1-yn-1-yl)phenyl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Mycobacterium tuberculosis
pH 7.0, 37°C
0.02858
eugenol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00108
isatin
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.02638
menthol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.01563
N-[(3-(2-amino-3-cyano-2H-benzo[h]chromen-4-y))phenyl]methylidyne]-2-hydroxyethanaminium
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0231
o-Cresol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0116
p-cymene
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0284
Thymol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0248
Vanillin
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0197
2-chloro-3-(5,6-difluoro-1H-indol-3-yl)quinoxaline
Mycobacterium tuberculosis
pH 7.0, 37°C
0.01974
2-chloro-3-(5,6-difluoro-1H-indol-3-yl)quinoxaline
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0198
3-(3-methoxyphenyl)-5,6,7,8-tetrahydrobenzo[b]thieno[2,3d]pyrimidin-4[3H]-one
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0198
3-(3-methoxyphenyl)-5,6,7,8-tetrahydrobenzo[b]thieno[2,3d]pyrimidin-4[3H]-one
Mycobacterium tuberculosis
pH 7.0, 37°C
0.01563
3-amino-1-(3-(4-hydroxybut-1-yn-1-yl)phenyl)-1H-benzol[f]chromene-2-carbonitril
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.01563
3-amino-1-(3-(4-hydroxybut-1-yn-1-yl)phenyl)-1H-benzol[f]chromene-2-carbonitril
Mycobacterium tuberculosis
pH 7.0, 37°C
0.01513
5-naphthyl-7-propyl-3H-pyrazolo-[4,3-d][1,2,3]triazin-4[5h]-one
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.01513
5-naphthyl-7-propyl-3H-pyrazolo-[4,3-d][1,2,3]triazin-4[5h]-one
Mycobacterium tuberculosis
pH 7.0, 37°C
0.007
Saccharomyces cerevisiae chorismate mutase inhibitors
Mycobacterium tuberculosis
(3S,6Z)-8-hydroxy-2-oxabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
1.2
Saccharomyces cerevisiae chorismate mutase inhibitors
Mycobacterium tuberculosis
(3S,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme activity in presence of amino acid effectors, overview
additional information
enzyme activity in presence of amino acid effectors, overview
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
additional information
enzyme activity in presence of amino acid effectors, overview
additional information
enzyme activity in presence of amino acid effectors, overview
additional information
enzyme activity in presence of amino acid effectors, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
6.6 - 7
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
5 - 9
the catalytic efficiency (kcat/Km) of *MtCM increases by two orders of magnitude upon decreasing the pH from 9 to 5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
70
-
As the temperature is lowered, distances of electrostatic and hydrophobic interactions decrease. The distance between Glu77-COOH and the hydroxyl oxygen decreases from the optimum
additional information
-
The average structures of the thermophilic E.S complex at three different temperatures are obtained from the MD simulations. A snapshot of the most important features of the active site of the TtCM E.S complex at 70°C is shown. At this temperature the Boltzmann distribution is primarily composed of reactive conformers - near attack conformers (NACs). The effects of the different temperatures on the distances in the structure are shown. The distances between electrostatic and hydrophobic pairs decrease as temperature decreases
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 70
-
studies that elucidate the dependence of the E-S active site on temperatures 25, 60 and 70°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme: chorismate mutase/prephenate dehydratase
-
-
brenda
Anthophyta
contain 3 isoenzymes with the exception of some closely related Leguminosae
-
-
brenda
strain 23 and its derivatives have 3 distinct enzyme species: CM1, CM2, and CM3. Strain 168 has only the CM3 form. Enzyme forms CM1 and CM2 may represent different aggregation states involving at least one common subunit
-
-
brenda
nonpathogenic species, Analysis of promoter activity described
Swissprot
brenda
i.e. Paraburkholderia phymatum, identified from root-nodule isolates from tropical legumes and is capable of symbiotic nitrogen fixation with the legumes Machaerium lunatum and Mimosa pudica
UniProt
brenda
Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815
i.e. Paraburkholderia phymatum, identified from root-nodule isolates from tropical legumes and is capable of symbiotic nitrogen fixation with the legumes Machaerium lunatum and Mimosa pudica
UniProt
brenda
bifunctional enzyme: chorismate mutase/prephenate dehydratase
-
-
brenda
bifunctional enzyme, catalyzes reactions of EC 2.5.1.54 and EC 5.4.99.5
UniProt
brenda
strain 23 and its derivatives have 3 distinct enzyme species: CM1, CM2, and CM3. Strain 168 has only the CM3 form. Enzyme forms CM1 and CM2 may represent different aggregation states involving at least one common subunit
-
-
brenda
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
brenda
bifunctional enzyme, catalyzes reactions of EC 2.5.1.54 and EC 5.4.99.5
UniProt
brenda
bifunctional chorismate mutase/prephenate dehydratase, cf. EC 4.2.1.51
Uniprot
brenda
bifunctional enzyme chorismate mutase/prephenate dehydratase
-
-
brenda
mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu
-
-
brenda
2 enzyme forms: chorismate mutase P and chorismate mutase T. Chorismate mutase P is associated with prephenate dehydratase, chorismate mutase T is associated with prephenate dehydrogenase
-
-
brenda
recombinant protein coded by the open reading frame Rv0948
-
-
brenda
recombinant protein coded by the open reading frame Rv1885c
-
-
brenda
Sequence data for Mycobacterium tuberculosis H37Rv and Mycobacterium leprae TN were obtained from the TubercuList (http://genolist.pasteur.fr/TubercuList/) and Leproma (http://genolist.pasteur.fr/Leproma/) databases; intracellular pathogen, studies of construction of mycobacterial reporter plasmids, organization of Rv0948c and Rv1885c promoter region, analysis of promoter activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
subventral and dorsal pharyngeal glands
brenda
-
the major fraction is formed by enzyme form CM2
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
identification of a chloroplast transit peptide
brenda
isoform CM1 is localized to the chloroplast stroma
brenda
identification of a chloroplast transit peptide
brenda
-
-
Rv0948c, the presence of a cleavable signal peptide in Rv1885c strongly suggests that they are exported
-
brenda
MtCM is secreted out of the cell to provide support to Mycobacterium tuberculosis in aromatic amino acid deficient medium
-
brenda
-
Mycobacterium tuberculosis enzyme has been shown to be secreted into the extracellular medium
-
brenda
absence of a discrete periplasmic compartment in Mycobacterium tuberculosis. *MtCM is secreted out of the cytoplasm and through the unusual architecture of the mycobacterial cell wall
-
brenda
-
MtCM is secreted out of the cell to provide support to Mycobacterium tuberculosis in aromatic amino acid deficient medium
-
-
brenda
-
absence of a discrete periplasmic compartment in Mycobacterium tuberculosis. *MtCM is secreted out of the cytoplasm and through the unusual architecture of the mycobacterial cell wall
-
-
brenda
isoform CM1 is imported into the plastid and processed to a mature size
brenda
additional information
-
the Mi-CM-3 probably functions within the cytoplasm of the host plant cell during nematode parasitism
-
brenda
additional information
-
Only one of the gene products is secreted into the extracellular space. This observation strongly suggests that while the cytosolic enzyme might have retained its role in the aromatic amino acid synthesis pathway, the secreted enzyme is likely to have evolved a distinct role, such as aiding the bacterium in its pathogenesis
-
brenda
additional information
isoform CM2 does not enter the plastid and is most likely not located in the chloroplast
-
brenda
additional information
isoform CM2 does not enter the plastid and is most likely not located in the chloroplast
-
brenda
additional information
-
isoform CM2 does not enter the plastid and is most likely not located in the chloroplast
-
brenda
additional information
enzyme SmCM is not predicted to have a chloroplast signal peptide
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
malfunction
metabolism
physiological function
additional information
drug target
the chorismate mutase is considered as an attractive target for the identification of potential antitubercular agents due to its absence in animals but not in bacteria
drug target
-
potential targets for developing virulence inhibitors against Acidovorax citrulli, a plant pathogenic bacterium that causes bacterial fruit blotch in cucurbit crops
drug target
chorismate mutase is known to be present in bacteria, fungi and higher plants but not in human
drug target
-
the chorismate mutase is considered as an attractive target for the identification of potential antitubercular agents due to its absence in animals but not in bacteria
-
drug target
-
chorismate mutase is known to be present in bacteria, fungi and higher plants but not in human
-
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
evolution
primitive molten globular enzymes might, like mMjCM, have had substantial advantages in forming stronger transition state interactions, since they could be more effective to explore different conformational states favorable to tighter binding of transition state
evolution
there are two classes of chorismate mutase: AroQ and AroH. The bacterial subclass AroQgamma has reported roles in virulence. Chorismate mutase from Burkholderia phymatum has the prototypical AroQgamma topology and retains the characteristic chorismate mutase active site
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
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
evolution
isozyme MtbCM belongs to the ?AroQ/AroQc family. The family members exhibit sequence similarity only in the N-terminal moiety, and lack a catalytically crucial and conserved arginine residue in helix H1. The proteins contain a catalytic site which is formed within a single protomer and lacks regulatory domain
evolution
-
chorismate mutase is highly conserved between plant-associated beta and gamma proteobacteria including phytopathogens belonging to the Xanthomonadaceae family
evolution
chorismate mutase is known to be present in bacteria, fungi and higher plants but not in human
evolution
-
chorismate mutase Mi-CM-3 is more similar to chorismate mutases from bacteria than to its paralogues identified in Meloidogyne incognita
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
-
evolution
-
chorismate mutase is known to be present in bacteria, fungi and higher plants but not in human
-
evolution
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
isozyme MtbCM belongs to the ?AroQ/AroQc family. The family members exhibit sequence similarity only in the N-terminal moiety, and lack a catalytically crucial and conserved arginine residue in helix H1. The proteins contain a catalytic site which is formed within a single protomer and lacks regulatory domain
-
evolution
Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815
-
there are two classes of chorismate mutase: AroQ and AroH. The bacterial subclass AroQgamma has reported roles in virulence. Chorismate mutase from Burkholderia phymatum has the prototypical AroQgamma topology and retains the characteristic chorismate mutase active site
-
malfunction
-
single-cell transient-induced gene silencing of CM1 in mildew resistance locus a (Mla) compromised cells results in increased susceptibility to Blumeria graminis f. sp. hordei
malfunction
-
Xanthomonas oryzae pv. oryzae chorismate mutase knock-out mutants are hypervirulent to rice
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
malfunction
compared to wild-type enzyme, decreased levels of Tparo7 expression in the silenced transformants are accompanied by reduced chorismate mutase activity, lower growth rates on different culture media, and reduced mycoparasitic behavior against the phytopathogenic fungi Rhizoctonia solani strain 19, Fusarium oxysporum strain CECT 2866, and Botrytis cinerea strain B05.10 in dual cultures. By contrast, higher amounts of the aromatic metabolites tyrosol, 2-phenylethanol and salicylic acid are detected in supernatants from the silenced transformants, which are able to inhibit the growth of Fusarium oxysporum and Botrytis cinerea. In in vitro plant assays, Tparo7-silenced transformants also show a reduced capacity to colonize tomato roots. The growth of tomato plants colonized by the silenced transformants is reduced and the plants exhibit an increased susceptibility to Bortrytis cinerea in comparison with the responses observed for control plants. In addition, the plants turn yellowish and are defective in jasmonic acid- and ethylene-regulated signaling pathways which is seen by expression analysis of lipoxygenase 1 (LOX1), ethylene-insensitive protein 2 (EIN2) and pathogenesis-related protein 1 (PR-1) genes
malfunction
the inhibition of secretory isozyme MtbCM may hinder the supply of nutrients to the organism
malfunction
-
Acidovorax citrulli strain lacking the bifunctional chorismate mutase/prephenate dehydratase (CmpAc, cf. EC 4.2.1.51), are significantly less virulent on watermelon in the germinated seed inoculation and leaf infiltration assays. The strain shows reduced twitching halo production and enhanced biofilm formation. the strain is less tolerant to osmotic stress but more tolerant to antibiotics (polymyxin B)
malfunction
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
the inhibition of secretory isozyme MtbCM may hinder the supply of nutrients to the organism
-
malfunction
Trichoderma parareesei IMI 113135 / T6
-
compared to wild-type enzyme, decreased levels of Tparo7 expression in the silenced transformants are accompanied by reduced chorismate mutase activity, lower growth rates on different culture media, and reduced mycoparasitic behavior against the phytopathogenic fungi Rhizoctonia solani strain 19, Fusarium oxysporum strain CECT 2866, and Botrytis cinerea strain B05.10 in dual cultures. By contrast, higher amounts of the aromatic metabolites tyrosol, 2-phenylethanol and salicylic acid are detected in supernatants from the silenced transformants, which are able to inhibit the growth of Fusarium oxysporum and Botrytis cinerea. In in vitro plant assays, Tparo7-silenced transformants also show a reduced capacity to colonize tomato roots. The growth of tomato plants colonized by the silenced transformants is reduced and the plants exhibit an increased susceptibility to Bortrytis cinerea in comparison with the responses observed for control plants. In addition, the plants turn yellowish and are defective in jasmonic acid- and ethylene-regulated signaling pathways which is seen by expression analysis of lipoxygenase 1 (LOX1), ethylene-insensitive protein 2 (EIN2) and pathogenesis-related protein 1 (PR-1) genes
-
metabolism
-
transgenic Arabidopsis plants expressing a truncated, feedback-insensitive chorismate mutase/prephenate dehydratase gene accumulate Phe (up to 100fold compared to control plants) and are more sensitive than wild-type plants to the Trp biosynthesis inhibitor 5-methyl-Trp. Thus Phe biosynthesis competes with Trp biosynthesis from their common precursor chorismate. A number of secondary metabolites derived from all three aromatic amino acids (Phe, Trp and Tyr) are altered in the transgenic plants, implying regulatory cross-interactions between the flux of aromatic amino acid biosynthesis from chorismate and their further metabolism into various secondary metabolites. Truncated PheA expression has a minimal effect on primary metabolism and on the Arabidopsis transcriptome. A high proportion of the feedback-insensitive chorismate mutase/prephenate dehydratase polypeptide produced by this transgene is translocated into the plastids
metabolism
-
chorismate mutase is the first and the key enzyme that diverges the shikimate pathway to either tryptophan or phenylalanine and tyrosine
metabolism
the enzyme is involved in aromatic amino acid biosynthesis
metabolism
the enzyme is involved in L-phenylalanine biosynthesis pathway
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
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
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
metabolism
chorismate mutase is located at the branch point of the shikimate pathway and channels chorismate into the Tyr/Phe-specific branch. The enzyme catalyzes the conversion of chorismate to prephenate
metabolism
the enzyme plays a central branch point role in the shikimate pathway, pathway and regulation, overview
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
metabolism
Mycobacterium tuberculosis chorismate mutase (MtbCM) catalyzes the rearrangement of chorismate to prephenate in the shikimate biosynthetic pathway which forms the essential amino acids, phenylalanine and tyrosine
metabolism
the chorismate mutase from Erysiphe quercicola can fully complement a Saccharomyces cerevisiae ScAro7 mutant that is deficient in the synthesis of phenylalanine and tyrosine
metabolism
-
shikimate pathway enzyme, plays a key role in the biosynthesis of aromatic compounds
metabolism
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
Mycobacterium tuberculosis chorismate mutase (MtbCM) catalyzes the rearrangement of chorismate to prephenate in the shikimate biosynthetic pathway which forms the essential amino acids, phenylalanine and tyrosine
-
metabolism
Trichoderma parareesei IMI 113135 / T6
-
the enzyme plays a central branch point role in the shikimate pathway, pathway and regulation, overview
-
metabolism
Corynebacterium glutamicum ATCC 25618
-
shikimate pathway enzyme, plays a key role in the biosynthesis of aromatic compounds
-
physiological function
isoform CM1 is the principal chorismate mutase responsible for the coupling of metabolites from the shikimate pathway to the synthesis of floral volatile benzenoid/phenylpropanoids in the corolla
physiological function
-
CM0819 significantly stimulates 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DS2098) activity, CM0819 interacts with 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase DS2098 from Corynebacterium glutamicum and this interaction results in allosteric regulation of DS2098 synthase activity
physiological function
-
isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform a nonphysiological role as a chorismate mutase albeit with considerably lower catalytic efficiency
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
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
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
physiological function
isozyme AtCM1 is alosterically regulated
physiological function
AtCM2 is a nonallosteric form
physiological function
isozyme AtCM3 is alosterically regulated
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
physiological function
enzyme chorismate mutase is a shikimate pathway branch point leading to the production of aromatic amino acids, which are not only essential components of protein synthesis but also the precursors of a wide range of secondary metabolites
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
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
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
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 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
Mycobacterium tuberculosis chorismate mutase (MtbCM) catalyzes the rearrangement of chorismate to prephenate in the shikimate biosynthetic pathway which forms the essential amino acids, phenylalanine and tyrosine. The secretory isozyme MtbCM (encoded by gene Rv1885c) is assumed to play a key role in pathogenesis of tuberculosis. Isozyme MtbCM is independent of regulation
physiological function
expression in Escherichia coli can complement the lack chorsimate mutase activity in a CM-deficient Escherchia coli strain. Rice plants constitutively expressing Hirschmanniella oryzae chorismate mutase or isochorismatase are more susceptible to H. oryzae infection due to down-regulation of genes involved in plant defence. Expression of chorismate mutase increases rice susceptibility against the sedentary nematode Meloidogyne graminicola also
physiological function
Hirschmanniella oryzae is one of the most devastating nematodes on rice, leading to substantial yield losses. The immune system of the host is altered by lowering secondary metabolite content upon secretion of chorismate mutase and isochorismatase
physiological function
-
key enzyme of the shikimate pathway regulating plant immunity. The secreted chorismate mutase attenuates virulence and walnut blight symptoms
physiological function
-
key enzyme in the biosynthesis of aromatic amino acids
physiological function
bacterial bifunctional chorismate mutase-prephenate dehydratase PheA increases flux into the yeast phenylalanine pathway
physiological function
plant pathogens recruit classically secreted chorismate mutase as an effector to disrupt plant salicylic acid synthesis
physiological function
key enzyme in the shikimate pathway responsible for the generation of aromatic amino acids
physiological function
-
key enzyme in the shikimate pathway. It produces aromatic amino acids. Auxotrophic assays demonstrate that the bifunctional chorismate mutase/prephenate dehydratase (CmpAc, cf. EC 4.2.1.51) is required for the biosynthesis of phenylalanine, but not tyrosine. The comparative proteomic analysis revealed that CmpAc is mostly involved in cell wall/membrane/envelop biogenesis
physiological function
-
Meloidogyne incognita manipulates plant cell development and metabolism by injecting effectors from the oesophageal glands into the plant host. Chorismate mutase (CM) is one such effector that may contribute to successful parasitism by Meloidogyne incognita. Chorismate mutase Mi-CM-3 may play an important role in suppressing plant immunity by regulating the salicylic acid pathway during the early parasitic stage of M. incognita so as to promote nematode parasitism
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
-
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
-
key enzyme in the shikimate pathway responsible for the generation of aromatic amino acids
-
physiological function
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
Mycobacterium tuberculosis chorismate mutase (MtbCM) catalyzes the rearrangement of chorismate to prephenate in the shikimate biosynthetic pathway which forms the essential amino acids, phenylalanine and tyrosine. The secretory isozyme MtbCM (encoded by gene Rv1885c) is assumed to play a key role in pathogenesis of tuberculosis. Isozyme MtbCM is independent of regulation
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physiological function
Trichoderma parareesei IMI 113135 / T6
-
enzyme chorismate mutase is a shikimate pathway branch point leading to the production of aromatic amino acids, which are not only essential components of protein synthesis but also the precursors of a wide range of secondary metabolites
-
physiological function
Paracidovorax citrulli KACC17005
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key enzyme in the shikimate pathway. It produces aromatic amino acids. Auxotrophic assays demonstrate that the bifunctional chorismate mutase/prephenate dehydratase (CmpAc, cf. EC 4.2.1.51) is required for the biosynthesis of phenylalanine, but not tyrosine. The comparative proteomic analysis revealed that CmpAc is mostly involved in cell wall/membrane/envelop biogenesis
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additional information
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structure-function relationships of chorismate-utilizing enzymes, structure comparisons, overview
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
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
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
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
enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
additional information
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enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
additional information
wild-type and molten globular chorismate mutase achieve comparable catalytic rates using very different enthalpy/entropy compensations, analysis using ab initio quantum mechanical/molecular mechanical minimum free-energy path method, overview. Site-specific, non-uniform rigidity changes of the enzymes during catalysis. The change of conformational entropy from the ground state to the transition state revealed distinctly contrasting entropy/enthalpy compensations in the dimeric wild-type enzyme and its molten globular monomeric variant. Molecular dynamics simulations
additional information
the enzyme is a chorismate mutase with AroQgamma topology, enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
additional information
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the enzyme is a chorismate mutase with AroQgamma topology, enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, 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
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
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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
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additional information
-
AroH molecular docking, using crystal structure of BsAroH, PDB ID 2CHT, overview
-
additional information
Burkholderia thailandensis ATCC 700388 / DSM 13276 / CIP 106301 / E264
-
enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
-
additional information
Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815
-
the enzyme is a chorismate mutase with AroQgamma topology, enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
-
Show AA Sequence and Transmembrane Helices (21442 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10090
90-MtCM, MALDI-TOF mass spectrometry and calculated from amino acid sequence
11770
105-MtCM, MALDI-TOF mass spectrometry and calculated from amino acid sequence
140000
-
chorismate mutase/prephenate dehydratase, enzyme form CM2, gel filtration
14500
18600
18747
2 * 18747, all alpha-helical bundle structure, two monomeric subunits
19540
19670
30000
Q9Y7B2
alpha2, 2 * 30000, calculated from amino acid sequence, homology modeling, electron microscopy
37000
monomeric molecular mass 18474 Da. Absorbance, liquid chromatography-mass spectrometry
40000
45000
50000
55000
56000
60000
65000
91000
-
gel filtration, in presence of Phe or Tyr a MW of 175000 is measured
14500
-
x * 14500, at least 3 subunits not linked together by disulfide bridges, SDS-PAGE
18600
-
monomer, mass spectrometry, 167-residue untagged lederless MtCM
19540
-
monomer, calculated from the variant that lacks 33 N-terminal residues
19670
-
monomer, mass, spectrometry, leaderless variant with additional start methionine
19670
-
monomer, calculated from the leaderless variant with additional start methionine
40000
-
x * 40000, the smallest native species of the enzyme, determined by sedimentation equilibrium, appears to be a dimer
40000
-
x * 40000, chorismate mutase/prephenate dehydratase, tryptic fingerprinting suggests that the 40000 MW subunits are closely similar if not identical
60000
about, recombinant detagged enzyme, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homohexamer
monomer
trimer
additional information
?
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x * 40000, the smallest native species of the enzyme, determined by sedimentation equilibrium, appears to be a dimer
?
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x * 40000, chorismate mutase/prephenate dehydratase, tryptic fingerprinting suggests that the 40000 MW subunits are closely similar if not identical
?
-
x * 14500, at least 3 subunits not linked together by disulfide bridges, SDS-PAGE
?
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x * 14500, at least 3 subunits not linked together by disulfide bridges, SDS-PAGE
-
?
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two different components are detected by gel filtration, component A with MW 250000 and component B with MW 25000. The two components associate reversibly to give an active enzyme complex with MW 320000
dimer
in the BsCM_2-chlorogenic acid structure, two active sites, S1 and S2, are located at the interface of two monomers
dimer
-
in the BsCM_2-chlorogenic acid structure, two active sites, S1 and S2, are located at the interface of two monomers
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dimer
-
the dimeric chorismate mutase is a thermostable and conventionally folded enzyme, X-ray chrystallography
dimer
Each assymmetric unit contains a homodimer, corresponding to the two protomers (A and B) of the biological dimer. The structure of a *MtCM protomer strongly resembles the fold of the EcCM dimer, which consists of two intertwined subunits of three helices each and which comprises two active sites
dimer
-
Each assymmetric unit contains a homodimer, corresponding to the two protomers (A and B) of the biological dimer. The structure of a *MtCM protomer strongly resembles the fold of the EcCM dimer, which consists of two intertwined subunits of three helices each and which comprises two active sites
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homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
homodimer
Q9Y7B2
alpha2, 2 * 30000, calculated from amino acid sequence, homology modeling, electron microscopy
homodimer
alpha2, 2 * 11883-11887, deduced from amino acid sequence, ESI-MS, MALDI-MS
homodimer
-
alpha2, 2 * 12843-12848, deduced from amino acid sequence, ESI-MS, MALDI-MS
homodimer
-
The regulating Trp ligand is found to be sandwiched between the two monomers in a dimer containing residues 66-68
homodimer
2 * 18747, all alpha-helical bundle structure, two monomeric subunits
homodimer
-
2 * 18747, all alpha-helical bundle structure, two monomeric subunits
-
homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
monomer
-
monomeric chorismate mutase combines high catalytic activity with the characteristics of a molten globule, X-ray crystallography
monomer
-
provides essentially the same catalytic power as the native enzyme, behaves like a molten globule (an ensemble of poorly packed and rapidly interconverting conformers)
additional information
the high-resolution structure of chorismate mutase is determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQgamma topology and shares conserved binding-cavity residues with other chorismate mutases. The AroQgamma topology is composed entirely of helices connected by short loops
additional information
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the high-resolution structure of chorismate mutase is determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQgamma topology and shares conserved binding-cavity residues with other chorismate mutases. The AroQgamma topology is composed entirely of helices connected by short loops
additional information
Burkholderia thailandensis ATCC 700388 / DSM 13276 / CIP 106301 / E264
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the high-resolution structure of chorismate mutase is determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQgamma topology and shares conserved binding-cavity residues with other chorismate mutases. The AroQgamma topology is composed entirely of helices connected by short loops
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additional information
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In MtbCM, while one face of helix 3 contributes to residues involved in monomer-monomer contracts and the allosteric site, the other face contributes to residues involved in the interaction with the substrate. The active site in the gene duplicated monomer is occupied by a sulfate ion and is located in the second half of the polypeptide
additional information
Ligand-induced structural changes are shown. Experiments neither show evidence for an equilibrium between the dimer and a *MtCM dimer of an intertwined nature, nor for an equilibrium with a monomer at lower protein concentrations as observed for engineered topology variants of chorismate mutases. The active site of *MtCM is highly similar to the catalytic sites of the other structurally characterized AroQ chorismate mutases
additional information
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Ligand-induced structural changes are shown. Experiments neither show evidence for an equilibrium between the dimer and a *MtCM dimer of an intertwined nature, nor for an equilibrium with a monomer at lower protein concentrations as observed for engineered topology variants of chorismate mutases. The active site of *MtCM is highly similar to the catalytic sites of the other structurally characterized AroQ chorismate mutases
additional information
secretory isozyme MtbCM undergoes dimerization mediated through residues (90-119) spanning H3 in both subunits, with the two helices placed anti parallel to each other. The polypeptide consists of eight a-helices H-H8 connected by turns and loop segments
additional information
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secretory isozyme MtbCM undergoes dimerization mediated through residues (90-119) spanning H3 in both subunits, with the two helices placed anti parallel to each other. The polypeptide consists of eight a-helices H-H8 connected by turns and loop segments
additional information
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
secretory isozyme MtbCM undergoes dimerization mediated through residues (90-119) spanning H3 in both subunits, with the two helices placed anti parallel to each other. The polypeptide consists of eight a-helices H-H8 connected by turns and loop segments
-
additional information
-
Ligand-induced structural changes are shown. Experiments neither show evidence for an equilibrium between the dimer and a *MtCM dimer of an intertwined nature, nor for an equilibrium with a monomer at lower protein concentrations as observed for engineered topology variants of chorismate mutases. The active site of *MtCM is highly similar to the catalytic sites of the other structurally characterized AroQ chorismate mutases
-
additional information
the enzyme is a chorismate mutases with AroQgamma topology
additional information
-
the enzyme is a chorismate mutases with AroQgamma topology
additional information
Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815
-
the enzyme is a chorismate mutases with AroQgamma topology
-
additional information
-
enzyme structure comparisons of isochorismate-pyruvate lyase, PchB, with chorismate mutases, overview
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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
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 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
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
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
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 400 nl of 20 mg/ml protein in 20 mM HEPES, pH 7.0, 300 mM NaCl, 5% glycerol, and 1 mM TCEP, with 400 nl reservoir solution containing 20% w/v PEG 3350, 200 mM ammonium nitrate, and equilibration against 0.08 ml of reservoir solution, 17°C, X-ray diffraction structure determination and analysis at 2.15 A resolution
crystal structures of the chorismate mutase homodimer and the heterooctameric chorismate mutase/CgDS complex, refined to 1.1 and 2.2 A resolution, respectively
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*MtCM, encoded by ORF Rv1885c in strain H37Rv. First characterized example of an AroQgamma fold. Description of the crystal optimization of a protein target that crystallizes very rapidly. 1. 175-residue version of *MtCM (encoded on plasmid pKTU3-HCT, dissolved in 20 mM potassium phosphate buffer pH7.5. 2. leaderless untagged 167-residue version of *MtCM encoded by plasmid pKTU3-HT used, buffered with 20 mM Tris-HCl pH 8.0)
37.2 kDa. Each asymmetric unit contains a homodimer, corresponding to the two protomers of the biological dimer. *MtCM as a model system for the *AroQ subclass and determined its crystal structure at high resolution, both in its unliganded form and in complex with transition state analog (1S,3S,5R,6R)-6-hydroxy-4-oxabicyco[3.3.1]non-7-ene-1,3-dicarboxylic acid. Heavy-atom derivatives prepared. Successful heavy-atom compounds are lead (II) acetate and thallium (III) acetate
alone and in complex with 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, hanging drop vapor diffusion method, using 25% (w/v) PEG 1500 and 0.1 M MMT buffer (L-malic acid, MES, Tris) pH 8.0-9.0
Analysis of the structure shows a novel fold topology for the protein with a topologically rearranged helix containing R134. *MtCM does not have an allosteric regulation site
analysis reveals the presence of two monomers in the asymmetric unit
-
in complex with L-malate, hanging drop vapor diffusion method, using 15% (w/v) PEG 1500 and 0.1 M of the L-malate-containing MMT buffer system pH 8.0-9.0
MtCM (Rv1885c) (PDB ID-2F6L), docked conformation of (3S,6Z)-8-hydroxy-2-oxabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid, 4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid, and (3S,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid, (2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid in the catalytic site of MtCM x-ray crystal structure is shown
of the homodimeric chorismate mutase (Rv1885c). The crystal structure corresponds to the AroQ class CM of Mycobacterium tuberculosis. Determination of the crystal structure of the unique extracytoplasmic MtbCM in complex with its allosteric ligand, L-Trp. Se-Met MtbCM crystallizes in space group C2 in the presence of Trp. The Mycobacterium tuberculosis enzyme is an all-helical protein. Structural comparisons show that CMs from different organisms have envolved into two completely unrelated protein folds, suggesting separate evolutionary origins of the enzyme. On the basis of the structural fold adopted by the protein, CMs have been classified into the AroH and AroQ classes
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sitting drop vapour diffusion method, using 0.1 M Tris-HCl (pH 8.6), 0.2 M MgCl2, and 20% poly(ethylene glycol) 400 for the 90 amino acid enzyme 90-MtCM
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 400 nl of 22.4 mg/ml protein in 20 mM HEPES, pH 7.0, 300 mM NaCl, 5% glycerol, and 1 mM TCEP, with 400 nl reservoir solution containing 20% w/v PEG 3350, 200 mM ammonium formate, pH 6.6, and equilibration against 0.08 ml of reservoir solution, X-ray diffraction structure determination and analysis at 1.95 A resolution
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
crystal structure of the T state of the allosteric enzyme and comparison with the R state
-
crystal structure of wild-type enzyme cocrystallized with Trp and an endo-exabicyclic transition state analogue inhibitor, of wild-type enzyme cocrystallized with Tyr and the endo-oxabicyclic transition state analogue inhibitor and of the Thr226Ser mutant enzyme in complex with Trp
-
The corresponding positional fluctuations from the MD simulation are in good agreement with those obtained by X-ray crystallography
-
hanging drop vapour diffusion method, in 2 M ammonium sulfate, 0.1 M citrate/phosphate buffer, pH 4.2
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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
D233I
Q9Y7B2
little reduced regulatory range through tyrosine and tryptophan than wild-type enzyme
D233T
Q9Y7B2
strong reduced regulatory range through tyrosine and tryptophan than wild-type enzyme
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
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
DELTA102-285
-
hybrid of chorismate mutase and allosteric domain from P-protein without prephrenate dehydratase
I81L/V85I
reduced catalytic efficiency, alters packing against the hydrophobic ring face of the reacting molecule
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
Q88E
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
F77W
-
mutant exhibits decreased activity compared to the wild type enzyme
Q88N
-
mutant exhibits decreased activity compared to the wild type enzyme
R51Q
-
mutant exhibits decreased activity compared to the wild type enzyme
V35A
-
mutant exhibits decreased activity compared to the wild type enzyme
D69A
site directed mutagenesis constitute the catalytic site
E109A
site directed mutagenesis constitute the catalytic site
E109Q
site directed mutagenesis constitute the catalytic site
G86A
mutant shows reduced kcat and Km values compared to the wild type enzyme
K60A
site directed mutagenesis constitute the catalytic site
R134A
site directed mutagenesis constitute the catalytic site
R49A
site directed mutagenesis constitute the catalytic site
R72A
site directed mutagenesis constitute the catalytic site
T52P/V55D/L88D
kcat/KM is 12.9fold higher than wild-type value
V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88D/G89A/H90M
kcat/KM is 1025fold higher than wild-type value
V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88L/G89A/H90M
kcat/KM is 941fold higher than wild-type value
V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88N/G89A/H90M
kcat/KM is 1000fold higher than wild-type value
Y105A
site directed mutagenesis constitute the catalytic site
V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88D/G89A/H90M
-
kcat/KM is 1025fold higher than wild-type value
-
V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88L/G89A/H90M
-
kcat/KM is 941fold higher than wild-type value
-
V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88N/G89A/H90M
-
kcat/KM is 1000fold higher than wild-type value
-
G86A
-
mutant shows reduced kcat and Km values compared to the wild type enzyme
-
E23D
abolishes the substrate-induced homotrophic effect, but retains the effector-induced heterotrophic effecs, the coupling between helix 11 and helix 12 is weakened
I225T
-
mutant enzyme Ile225Thr is activated by Trp, but is insensitive to Tyr
T226D
-
reduced regulatory range through tyrosine and tryptophan than wild-type enzyme
T226I
Y234F
-
enzymes with mutations of Tyr234, especially Tyr234Phe are unresponsive to Tyr but are activated by Trp
additional information
DELTA117-127
-
large increase in KM and slower turnover relative to 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
T226I
-
reduced regulatory range through tyrosine and tryptophan than wild-type enzyme
additional information
-
-
CM enzymes, which are not precisely annotated in the original genome sequence of Mycobacterium tuberculosis H37Rv and the subsequent reannotation. In the annotation, two ORFs (Rv0948c and Rv1885) with some similarity to CMs, including the well-known monofunctional periplasmic CM from Erwinia herbicola, are found, although these ORFs are described as conserved hypothetical proteins
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
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
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
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
Gr-cm-1-IRII, generated by retention of intron 2 of the Gr-cm-1 pre-mRNA through alternative splicing encodes a truncated protein (GR-CM-1t) lacking the chorismate mutase domain with no activity
additional information
-
Gr-cm-1-IRII, generated by retention of intron 2 of the Gr-cm-1 pre-mRNA through alternative splicing encodes a truncated protein (GR-CM-1t) lacking the chorismate mutase domain with no activity
additional information
The results of the mutagenesis and the activity show that Arg49, Lys 60, Arg72, and Arg134 are essential for catalysis
additional information
-
The results of the mutagenesis and the activity show that Arg49, Lys 60, Arg72, and Arg134 are essential for catalysis
additional information
silencing of gene Tparo7, mutant phenotype, plant rhizosphere colonization tests on tomato plants, detailed overview
additional information
-
silencing of gene Tparo7, mutant phenotype, plant rhizosphere colonization tests on tomato plants, detailed overview
additional information
Trichoderma parareesei IMI 113135 / T6
-
silencing of gene Tparo7, mutant phenotype, plant rhizosphere colonization tests on tomato plants, detailed overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
30
42
-
4 min, 59% loss of chorismate mutase P activity, no effect on chorismate mutase T activity
45
52
58
-
1 h, 50% inactivation, genetically engineered enzyme with amino acid residues 1-285
60
62
-
1 h, 50% inactivation, genetically engineered enzyme with amino acid residues 1-300
additional information
60
-
complete denaturation of the enzyme occurs at a temperature close to 60°C
60
isozyme MtCM meltig temperature is 48°C, complete inactivation at 60°C
additional information
The melting point of the active complementations (changes in position 7, 32, 35, 48, 81 and 85) is shown
additional information
-
The melting point of the active complementations (changes in position 7, 32, 35, 48, 81 and 85) is shown
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
chorismate mutase irreversibly immobilized by n-decylamine-substituted agarose allows repeated quantitative conversion of chorismate to prephenate
-
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+
-
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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
-
4°C, 0.1 mM Trp, stable for 5 days with a rapid loss in activity after this time
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
*MtCM, which has a melting temperature of 48°C, rapidly renatures after heat denaturation, and have subsequently exploited this feature for purifying the enzyme
ammonium sulfate precipitation, Ni-NTA agarose column chromatography, and Superdex 75 gel filtration
anion exchange column chromatography, Superdex 75 gel filtration
AtCM1, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta II (DE3)
enzyme form CM1 and CM2
partial
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)-R3 Rosetta by nickel affinity chromatography, gel filtration, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)R3 Rosetta by nickel affinity chromatography, gel filtration, and ultrafiltration
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
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
subtilisin column chromatography and Sephadex G-75 gel filtration
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
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
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtCM1, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta II (DE3)
AtCM3, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta II (DE3)
Construction of mycobacterial reporter plasmids is described. In contrast to the studies in Mycobacterium tuberculosis, very little is known of CMs in Mycobacterium smegmatis. Homolouges of Rv1885c and Rv0948c are present in the MSMEG5513 have been recently annotated as potential CMs. Rv1885c protein used as a control for the experiments describing Rv0948c and the two Mycobacterium smegmatis homologues
Escherichia coli strains C600lambda lysogen, MZ1, Nova Blue, BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain KA13
expression in Escherichia coli
gene Bphy_7813, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)-R3 Rosetta
gene BTH_I1596, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)R3 Rosetta
gene Tparo7, DNA and amino acid sequence determination and analysis, quantitative real-time PCR enzyme expression analysis
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
-
in Mycobacterium smegmatis: homologues of each CM from Mycobacterium tuberculosis are found in Mycobacterium smegmatis, a nonpathogenic species. These homologues (which correspond to ORFs MSMEG5513 and MSMEG2114 respectively) cloned, expressed in Escherichia coli (strains DH5alpha, DH10B and BL21(DE3)), and demonstrate to possess CM activity as their Mycobacterium tuberculosis counterparts
overexpressed in Escherichia coli BL21 (DE3). Mycobacterium tuberculosis CMs are believed to have evolved from duplication of an ancestral CM gene, formation of the active site in a single polypeptide chain appears to be a consequence of this duplication event
-
overexpression in a Saccharomyces cerevisiae aro7DELTA mutant strain
Q9Y7B2
overexpression in Escherichia coli
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
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
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
the coding sequence of Mi-cm-3 without the native signal peptide is fused with GFP and transiently expressed in Nicotiana benthamiana leaves via agroinfiltration. Constitutive expression of Mi-CM-3 in plants affects normal root growth and promotes nematode parasitism
-
the Rv1885c gene product is synthesized with an N-terminal signal sequence of 33 amino acids, which is cleaved off upon heterologous expression in Escherichia coli, and transported into the periplasmic space
the transient expression of chorismate mutase from Erysiphe quercicola in Nicotiana benthamiana leaf tissues can promote infection by Phytophthora capsici and suppress plant levels of salicylic acid and salicylic acid mediated defense in response to Phytophthora capsici infection via chorismate mutase enzyme activity
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the ezyme is dramatically upregulated during penetration and haustoria formation
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme can be inactivated in a boiling water bath and afterwards reactivated at 30 C to 100% of its original activity
-
misfolded, higher-order aggregates convert into fully active dimeric protein by denaturation with guanidinium chloride and subsequent renaturation upon dilution into native buffer
thermal denaturation shows a sharp transition from the native to the denatured state, with a calculated Tm of 48°C. Upon subsequent cooling, the protein renatured easily
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
the widespread presence of chorismate mutases in the specialized sedentary endoparasitic nematode species suggests that this multifunctional enzyme may be a key factor in modulating plant parasitism
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
drug development
synthesis
drug development
-
the enzyme serves as a potential target for the development of inhibitors specific to the pathogen
drug development
multiple-drug-resistant tuberculoses bacillus and its synergism with HIV-characterization of new enzyme targets and the development of new drugs
drug development
-
MtCM might play a role in host-pathogen interactions, making it an important target for designing inhibitor molecules against the deadly pathogen
drug development
fighting diseases such as tuberculosis. Since vertebrates lack the shikimate pathway for the biosynthesis of aromatic compounds and thus do not possess chorismate mutase activity, this enzyme represents a prime target for the development of antibiotics, fungicides and herbicides
drug development
advantage of the nonoccurance of CMs in human, develop antimicrobial drugs to combat dreaded human pathogens such as Mycobacterium tuberculosis
drug development
-
-
Since this enzyme is absent from mammals, it represents a promising target for the development of new antimycobacterial drugs, which are needed to combat Mycobacterium tuberculosis, the causative agent of tuberculosis
drug development
since vertebrates lack the shikimate pathway for the biosynthesis of aromatic compounds and thus do not possess chorismate mutase activity, the enzyme represents a prime target for the development of antibacterials
drug development
the secretory isozyme is a target for the discovery of anti-tubercular agents
drug development
-
multiple-drug-resistant tuberculoses bacillus and its synergism with HIV-characterization of new enzyme targets and the development of new drugs
-
drug development
-
fighting diseases such as tuberculosis. Since vertebrates lack the shikimate pathway for the biosynthesis of aromatic compounds and thus do not possess chorismate mutase activity, this enzyme represents a prime target for the development of antibiotics, fungicides and herbicides
-
drug development
-
advantage of the nonoccurance of CMs in human, develop antimicrobial drugs to combat dreaded human pathogens such as Mycobacterium tuberculosis
-
drug development
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
the secretory isozyme is a target for the discovery of anti-tubercular agents
-
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
synthesis
expression of a feedback-resistant version of pheA together with hydroxymandelate synthase from a single plasmid in the aro7DELTA Saccharomyces cerevisiae strain MRY36 increases mandelic acid MA production 12fold. Mandelic acid is an important aromatic fine chemical
synthesis
engineering of a tyrosine prototrophic mandelic acid-producing Saccharomyces cerevisiae strain utilizing a feedback-resistant version of the bifunctional Escherichia coli enzyme PheA in an Aro7 deletion strain. Expression of PheA significantly reduces hydroxymandelic acid production in favor of increased mandelic acid production, without causing tyrosine auxotrophy. Mandelic acid production can be increased 12fold, yielding titers up to 120 mg/l
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Release 2026.1 (March 2026)
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