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Information on EC 4.2.99.21 - isochorismate lyase
for references in articles please use BRENDA:EC4.2.99.21
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EC Tree 4 Lyases
4.2 Carbon-oxygen lyases
4.2.99 Other carbon-oxygen lyases
4.2.99.21 isochorismate lyase
IUBMB Comments
This enzyme is part of the pathway of salicylate formation from chorismate, and forms an integral part of pathways that produce salicylate-derived siderophores, such as pyochelin and yersiniabactin.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 4.2.99.21
-
siderophore
-
pericyclic
-
chorismate-utilizing
- prephenate
- 2,3-dihydroxybenzoate
- anthranilate
-
mg2+-dependent
- enterobactin
- drug development
- agriculture
- biotechnology
- synthesis
showSynonyms
isochorismate pyruvate lyase, isochorismate-pyruvate lyase, isochorismate lyase, prxr1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
pyochelin biosynthetic protein PchB
-
-
-
-
IPL
Irp9
isochorismate pyruvate lyase
isochorismate-pyruvate lyase
MbtI
PchB
PRXR1
salicylate biosynthesis protein pchB
-
-
-
-
salicylate synthase
IPL
Arabidopsis thaliana ecotype Di-17
-
-
-
IPL
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
UniProt
-
isochorismate pyruvate lyase
-
-
-
-
isochorismate pyruvate lyase
Arabidopsis thaliana ecotype Di-17
-
-
-
isochorismate-pyruvate lyase
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
-
PchB
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
-
PRXR1
Arabidopsis thaliana ecotype Di-17
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isochorismate = salicylate + pyruvate
-
-
-
-
isochorismate = salicylate + pyruvate
[1,5]-sigmatropic reaction mechanism that invokes electrostatic catalysis in analogy to the [3,3]-pericyclic rearrangement of chorismate in chorismate mutase
-
isochorismate = salicylate + pyruvate
a reactive substrate conformation is formed upon loop closure of the active site and ordering of the loop contributes to the entropic penalty for converting the enzyme substrate complex to the transition state. The thermodynamic parameters of the physiological lyase activity of PchB show that the reaction is clearly enthalpically driven, and has a very large entropic penalty of 24.3 cal/(mol K), which is more than 1.5-fold greater than that of the uncatalyzed reaction of 15.77 cal/(mol K)
-
isochorismate = salicylate + pyruvate
reaction mechanism with catalytic residue Lys42, modeling, overview
-
isochorismate = salicylate + pyruvate
the enzyme achieves catalysis of both pericyclic reactions, isochorismate-pyruvate lyase and chorismate-pyruvate lyase, EC 4.1.3.40, in part by the stabilization of reactive conformations and in part by electrostatic transition-state stabilization. Both, substrate organization and electrostatic transition state stabilization, contribute to catalysis
isochorismate = salicylate + pyruvate
reaction mechanism, the IPL reaction is a concerted but asynchronous hydrogen transfer, by a proposed [1,5]-sigmatropic reaction mechanism with a pericyclic transition state, quantum mechanical/molecular-mechanical calculations and simulations, overview
-
isochorismate = salicylate + pyruvate
kinetic mechanism and transition state of the elimination reaction, overview
-
isochorismate = salicylate + pyruvate
the lysine42 residue is required in a specific conformation to stabilize the transition state
-
isochorismate = salicylate + pyruvate
overall reaction, salicylate sythase converts chorismate into salicylate via an isochorismate intermediate
-
isochorismate = salicylate + pyruvate
overall reaction, salicylate sythase converts chorismate into salicylate via an isochorismate intermediate
-
isochorismate = salicylate + pyruvate
overall reaction, salicylate sythase converts chorismate into salicylate via an isochorismate intermediate
isochorismate = salicylate + pyruvate
overall reaction, salicylate sythase converts chorismate into salicylate via an isochorismate intermediate. In the second reaction, pyruvate is eliminated through an intramolecular [3,3]-sigmatropic rearrangement, formerly a retro-Ene reaction, to afford salicylic acid via bicyclic transition state TS2
isochorismate = salicylate + pyruvate
overall reaction, salicylate sythase converts chorismate into salicylate via an isochorismate intermediate
-
-
isochorismate = salicylate + pyruvate
overall reaction, salicylate sythase converts chorismate into salicylate via an isochorismate intermediate. In the second reaction, pyruvate is eliminated through an intramolecular [3,3]-sigmatropic rearrangement, formerly a retro-Ene reaction, to afford salicylic acid via bicyclic transition state TS2
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PATHWAY SOURCE
PATHWAYS
MetaCyc
salicylate biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
isochorismate pyruvate-lyase (salicylate-forming)
This enzyme is part of the pathway of salicylate formation from chorismate, and forms an integral part of pathways that produce salicylate-derived siderophores, such as pyochelin and yersiniabactin.
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CAS REGISTRY NUMBER
COMMENTARY
383896-77-3
-
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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
isochorismate
salicylate + pyruvate
Arabidopsis thaliana ecotype Di-17
-
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
-
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
-
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
-
Substrates: elimination of pyruvate
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: elimination of pyruvate
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
-
Substrates: pericyclic reaction, elimination of pyruvate. The electrostatic field due to PchB at atoms of isochorismate favors the isochorismate to salicylate transition, molecular dynamics simulations, overview
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
-
Substrates: isochorismate undergoes elimination to form salicylate and pyruvate and rearrangement to form isoprephenate in the absence of enzyme
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
-
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: incubation of chorismate with the combination of the recombinant proteins EntC (isochorismate synthase, EC 5.4.4.2) and His-PRXR1 results in enhanced levels of salicylate, in a His-PRXR1-dependent manner
Products: -
Products: -
?
additional information
?
-
Arabidopsis thaliana ecotype Di-17
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Substrates: incubation of chorismate with the combination of the recombinant proteins EntC (isochorismate synthase, EC 5.4.4.2) and His-PRXR1 results in enhanced levels of salicylate, in a His-PRXR1-dependent manner
Products: -
Products: -
?
additional information
?
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Substrates: nucleophilic substitution reaction, enzyme is able to use H2O as a nucleophile. Catalytic base K147 is not solely responsible for activation of H2O as a nucleophile
Products: -
Products: -
?
additional information
?
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Substrates: isochorismate is a kinetically competent intermediate in the synthesis of salicylate from chorismate. At pH values below 7.5 isochorismate is the dominant product while above this pH value the enzyme converts chorismate to salicylate without the accumulation of isochorismate in solution. MbtI may exploit a sigmatropic pyruvate elimination mechanism
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
Products: -
Products: -
?
additional information
?
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Substrates: the 2H kinetic isotope effects on kcat and the ratio kcat/Km are 2.34 and 1.75, respectively. Chemistry is significantly rate-determining for the enzyme. The magnitude of the isotope effect is consistent with considerable C-H bond cleavage in the transition state. The significant 2H kinetic isotope effect and quantitative transfer of the label to pyruvate are both consistent with a pericyclic reaction mechanism
Products: -
Products: -
?
additional information
?
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Substrates: enzyme additionally catalyzes the rearrangement of chorismate into prephenate and shows chorismate mutase activity. Both transformation of isochorismate into pyruvate and salicylate and the rearrangement of chorismate into prephenate proceed via a pericyclic reaction mechanism
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?
additional information
?
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Substrates: PchB can also perform a nonphysiological role as a chorismate mutase, EC 4.1.3.40, albeit with considerably lower catalytic efficiency
Products: -
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?
additional information
?
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Substrates: PchB can also perform a nonphysiological role as a chorismate mutase albeit with considerably lower catalytic efficiency
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?
additional information
?
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Substrates: PchB can also perform a nonphysiological role as a chorismate mutase albeit with considerably lower catalytic efficiency
Products: -
Products: -
?
additional information
?
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Substrates: PchB possesses weak chorismate mutase activity as well and is able to catalyze two distinct pericyclic reactions in a single active site. The enzyme tends to bring its non-native substrate in the same conformation as its native substrate
Products: -
Products: -
?
additional information
?
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Substrates: isochorismate synthase PhA additionally shows isochorismate lyase activity. Site-specific mutation of active site residues promotes lyase activity
Products: -
Products: -
?
additional information
?
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Substrates: enzyme converts chorismate to salicylate. The reaction proceeds through the intermediate isochorismate
Products: -
Products: -
?
additional information
?
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Substrates: enzyme converts chorismate to salicylate. The reaction proceeds through the intermediate isochorismate
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?
additional information
?
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Substrates: enzyme directly converts chorismat into salicylate
Products: -
Products: -
?
additional information
?
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Substrates: salicylate synthase Irp9 additionally shows isochorismate lyase activity
Products: -
Products: -
?
additional information
?
-
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Substrates: the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
Products: -
Products: -
?
additional information
?
-
Substrates: salicylate synthase Irp9 additionally shows isochorismate lyase activity
Products: -
Products: -
?
additional information
?
-
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Substrates: the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
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
isochorismate
salicylate + pyruvate
Arabidopsis thaliana ecotype Di-17
-
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Substrates: -
Products: -
Products: -
?
isochorismate
salicylate + pyruvate
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
the salicylate and isochorismate synthase activities of MbtI are Mg2+-dependent, and in the absence of Mg2+, MbtI has a promiscuous chorismate mutase activity similar to that of the isochorismate pyruvate lyase, PchB, from Pseudomonas aeruginosa
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4R,5R)-5-(carboxymethoxy)-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(1R)-1-carboxyethoxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(1S)-1-carboxyethoxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(2-carboxyprop-2-en-1-yl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(E)-3-(1-carboxyprop-1-enyloxy)-2-hydroxybenzoic acid
-
low micromolar inhibition of both isochorismate lyase and anthranilate synthase
1-(2-sulfanylidene-2,3-dihydro-1H-benzimidazol-1-yl)ethan-1-one
-
3-(1-carboxy-2-phenylvinyloxy)-2-hydroxybenzoic acid
-
low micromolar inhibition of both isochorismate lyase and anthranilate synthase
3-(1-carboxy-3-methylbut-1-enyloxy)-2-hydroxybenzoic acid
-
low micromolar inhibition of both isochorismate lyase and anthranilate synthase
3-(1-carboxybut-1-enyloxy)-2-hydroxybenzoic acid
-
low micromolar inhibition of both isochorismate lyase and anthranilate synthase
3-([(E)-1-carboxy-2-[2-(trifluoromethyl)phenyl]ethenyl]oxy)-2-hydroxybenzoic acid
-
3-([(E)-1-carboxy-2-[3-(trifluoromethyl)phenyl]ethenyl]oxy)-2-hydroxybenzoic acid
-
3-([(E)-1-carboxy-2-[4-(trifluoromethyl)phenyl]ethenyl]oxy)-2-hydroxybenzoic acid
-
3-([(E)-2-[2-(acetyloxy)phenyl]-1-carboxyethenyl]oxy)-2-hydroxybenzoic acid
-
3-([(E)-2-[3-(acetyloxy)phenyl]-1-carboxyethenyl]oxy)-2-hydroxybenzoic acid
-
3-([(E)-2-[4-(acetyloxy)phenyl]-1-carboxyethenyl]oxy)-2-hydroxybenzoic acid
-
3-[(2-carboxyprop-2-en-1-yl)oxy]-4,5-dihydroxybenzoic acid
-
3-[[(1E)-1-carboxy-3-methylbut-1-en-1-yl]oxy]-4-hydroxybenzoic acid
-
3-[[(1E)-1-carboxy-3-methylbut-1-en-1-yl]oxy]benzoic acid
-
3-[[(1E)-1-carboxyprop-1-en-1-yl]oxy]-2-hydroxybenzoic acid
-
3-[[(1E)-1-carboxyprop-1-en-1-yl]oxy]-4-hydroxybenzoic acid
-
3-[[(E)-1-carboxy-2-(2-chlorophenyl)ethenyl]oxy]-2-hydroxybenzoic acid
-
3-[[(E)-1-carboxy-2-(2-methylphenyl)ethenyl]oxy]-2-hydroxybenzoic acid
-
3-[[(E)-1-carboxy-2-(3-chlorophenyl)ethenyl]oxy]-2-hydroxybenzoic acid
-
3-[[(E)-1-carboxy-2-(3-methylphenyl)ethenyl]oxy]-2-hydroxybenzoic acid
-
3-[[(E)-1-carboxy-2-(4-chlorophenyl)ethenyl]oxy]-2-hydroxybenzoic acid
-
3-[[(E)-1-carboxy-2-(4-methylphenyl)ethenyl]oxy]-2-hydroxybenzoic acid
-
3-[[(E)-1-carboxy-2-phenylethenyl]oxy]-2-hydroxybenzoic acid
-
3-[[(E)-1-carboxy-2-phenylethenyl]oxy]-4-hydroxybenzoic acid
-
3-[[(E)-2-(2-bromophenyl)-1-carboxyethenyl]oxy]-2-hydroxybenzoic acid
-
3-[[(E)-2-(3-bromophenyl)-1-carboxyethenyl]oxy]-2-hydroxybenzoic acid
-
3-[[(E)-2-(4-bromophenyl)-1-carboxyethenyl]oxy]-2-hydroxybenzoic acid
-
methyl 2-hydroxy-3-([(1E)-3-methoxy-3-oxo-1-[2-(trifluoromethyl)phenyl]prop-1-en-2-yl]oxy)benzoate
-
methyl 2-hydroxy-3-([(1E)-3-methoxy-3-oxo-1-[3-(trifluoromethyl)phenyl]prop-1-en-2-yl]oxy)benzoate
-
methyl 2-hydroxy-3-([(1E)-3-methoxy-3-oxo-1-[4-(trifluoromethyl)phenyl]prop-1-en-2-yl]oxy)benzoate
-
methyl 2-hydroxy-3-[[(1E)-3-methoxy-1-(2-methylphenyl)-3-oxoprop-1-en-2-yl]oxy]benzoate
-
methyl 2-hydroxy-3-[[(1E)-3-methoxy-1-(3-methylphenyl)-3-oxoprop-1-en-2-yl]oxy]benzoate
-
methyl 2-hydroxy-3-[[(1E)-3-methoxy-1-(4-methylphenyl)-3-oxoprop-1-en-2-yl]oxy]benzoate
-
methyl 3-([(1E)-1-[2-(acetyloxy)phenyl]-3-methoxy-3-oxoprop-1-en-2-yl]oxy)-2-hydroxybenzoate
-
methyl 3-([(1E)-1-[3-(acetyloxy)phenyl]-3-methoxy-3-oxoprop-1-en-2-yl]oxy)-2-hydroxybenzoate
-
methyl 3-([(1E)-1-[4-(acetyloxy)phenyl]-3-methoxy-3-oxoprop-1-en-2-yl]oxy)-2-hydroxybenzoate
-
methyl 3-[[(1E)-1-(2-bromophenyl)-3-methoxy-3-oxoprop-1-en-2-yl]oxy]-2-hydroxybenzoate
-
methyl 3-[[(1E)-1-(2-chlorophenyl)-3-methoxy-3-oxoprop-1-en-2-yl]oxy]-2-hydroxybenzoate
-
methyl 3-[[(1E)-1-(3-bromophenyl)-3-methoxy-3-oxoprop-1-en-2-yl]oxy]-2-hydroxybenzoate
-
methyl 3-[[(1E)-1-(3-chlorophenyl)-3-methoxy-3-oxoprop-1-en-2-yl]oxy]-2-hydroxybenzoate
-
methyl 3-[[(1E)-1-(4-bromophenyl)-3-methoxy-3-oxoprop-1-en-2-yl]oxy]-2-hydroxybenzoate
-
methyl 3-[[(1E)-1-(4-chlorophenyl)-3-methoxy-3-oxoprop-1-en-2-yl]oxy]-2-hydroxybenzoate
-
N-ethyl-3-(3-oxo-1,2-benzothiazol-2(3H)-yl)benzene-1-sulfonamide
-
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
inhibition of salicylate synthase activity
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
additional information
inhibitor structure-function realtionship and molecular docking; inhibitor structure-function relationship and molecular docking
-
additional information
-
not inhibitory at 1 mM: EDTA, EGTA, or o-phenanthroline. No substrate inhibition up to 1.2 mM
-
additional information
-
inhibitor structure-function realtionship and molecular docking; inhibitor structure-function relationship and molecular docking
-
additional information
-
inhibitor structure-function realtionship and molecular docking; inhibitor structure-function relationship and molecular docking
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Understanding the different activities of highly promiscuous MbtI by computational methods.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics and thermodynamics, overview
-
0.00058
isochorismate
wild-type, 25°C, pH not specified in the publication
0.00059
isochorismate
mutant T348A, 25°C, pH not specified in the publication
0.0017
isochorismate
mutant E281D, 25°C, pH not specified in the publication
0.011
isochorismate
-
mutant D310E/A375T, 25°C, pH not specified in the publication
0.012
isochorismate
-
mutant A375T, 25°C, pH not specified in the publication
0.0137
isochorismate
-
mutant D310E, 25°C, pH not specified in the publication
0.0156
isochorismate
-
mutant C7A/K42C, treatment with bromoethylamine, pH 8.0, 20°C
0.023
isochorismate
-
mutant K42C, treatment with bromoethylamine, pH 8.0, 20°C
0.042
isochorismate
-
wild-type, 25°C, pH not specified in the publication
0.047
isochorismate
mutant E281D/T348A, 25°C, pH not specified in the publication
0.048
isochorismate
-
mutant K42A, presence of propylamine, pH 8.0, 20°C
0.06
isochorismate
-
mutant K42A, presence of ethylamine, pH 8.0, 20°C
0.114
isochorismate
-
mutant C7A/K42C, treatment with bromoethanol, pH 8.0, 20°C
0.125
isochorismate
-
mutant K42C, treatment with bromoethanol, pH 8.0, 20°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00038
isochorismate
-
mutant D310E/A375T, 25°C, pH not specified in the publication
0.0004
isochorismate
-
mutant A375T, 25°C, pH not specified in the publication
0.00069
isochorismate
-
mutant D310E, 25°C, pH not specified in the publication
0.0007
isochorismate
-
wild-type, 25°C, pH not specified in the publication
0.0055
isochorismate
mutant T348A, 25°C, pH not specified in the publication
0.0128
isochorismate
-
mutant C7A/K42C, treatment with bromoethanol, pH 8.0, 20°C
0.0184
isochorismate
-
mutant K42C, treatment with bromoethanol, pH 8.0, 20°C
0.0343
isochorismate
mutant E281D/T348A, 25°C, pH not specified in the publication
0.05
isochorismate
mutant E281D, 25°C, pH not specified in the publication
0.083
isochorismate
-
mutant K42A, presence of ethylamine, pH 8.0, 20°C
0.092
isochorismate
wild-type, 25°C, pH not specified in the publication
0.0945
isochorismate
-
mutant K42C, treatment with bromoethylamine, pH 8.0, 20°C
0.098
isochorismate
-
mutant K42A, presence of propylamine, pH 8.0, 20°C
0.105
isochorismate
-
mutant C7A/K42C, treatment with bromoethylamine, pH 8.0, 20°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
isochorismate
-
wild-type, 25°C, pH not specified in the publication
0.0366
isochorismate
-
mutant A375T, 25°C, pH not specified in the publication
0.037
isochorismate
-
mutant D310E/A375T, 25°C, pH not specified in the publication
0.0504
isochorismate
-
mutant D310E, 25°C, pH not specified in the publication
0.103
isochorismate
-
mutant C7A/K42C, treatment with bromoethanol, pH 8.0, 20°C
0.147
isochorismate
-
mutant K42C, treatment with bromoethanol, pH 8.0, 20°C
0.74
isochorismate
mutant E281D/T348A, 25°C, pH not specified in the publication
1.37
isochorismate
-
mutant K42A, presence of propylamine, pH 8.0, 20°C
2.06
isochorismate
-
mutant K42A, presence of ethylamine, pH 8.0, 20°C
4.2
isochorismate
-
mutant K42C, treatment with bromoethylamine, pH 8.0, 20°C
6.7
isochorismate
-
mutant C7A/K42C, treatment with bromoethylamine, pH 8.0, 20°C
9.3
isochorismate
mutant T348A, 25°C, pH not specified in the publication
31
isochorismate
mutant E281D, 25°C, pH not specified in the publication
159
isochorismate
wild-type, 25°C, pH not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
(E)-3-(1-carboxyprop-1-enyloxy)-2-hydroxybenzoic acid
-
pH 8.0, 25°C
0.024
2-amino-3-(1-carboxyethoxy)benzoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.021
3-(1-carboxy-2-phenylvinyloxy)-2-hydroxybenzoic acid
-
pH 8.0, 25°C
0.014
3-(1-carboxy-3-methylbut-1-enyloxy)-2-hydroxybenzoic acid
-
pH 8.0, 25°C
0.012
3-(1-carboxybut-1-enyloxy)-2-hydroxybenzoic acid
-
pH 8.0, 25°C
0.019
3-(1-carboxyethoxy)-2-hydroxybenzoic acid
-
pH not specified in the publication, temperature not specified in the publication
1.4
3-(1-carboxyethoxy)-4,5-dihydroxybenzoic acid
pH and temperature not specified in the publication
1.7
3-[(1-carboxyethenyl)oxy]-4,5-dihydroxybenzoic acid
pH and temperature not specified in the publication
3
3-[(2-carboxyprop-2-en-1-yl)oxy]-4,5-dihydroxybenzoic acid
pH and temperature not specified in the publication
0.0001
4,4'-sulfonylbis(2,6-dinitrophenol)
pH and temperature not specified in the publication
0.00087
4,6-dinitro-2-oxo-1,3-benzoxathiol-5-yl methyl carbonate
pH and temperature not specified in the publication
0.025
4,6-dinitro-2-oxo-2H-1,3-benzoxathiol-5-yl methyl carbonate
-
pH and temperature not specified in the publication
0.043
4-amino-3-(1-carboxyethoxy)benzoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0001
5-[(2-carboxyphenyl)sulfamoyl]-2-hydroxybenzoic acid
pH and temperature not specified in the publication
0.16
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
pH and temperature not specified in the publication, inhibition of salicylate synthase activity
0.16
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
additional information
-
at pH values below 7.5 isochorismate is the dominant product while above this pH value the enzyme converts chorismate to salicylate without the accumulation of isochorismate in solution
4 - 9
active across the entire pH-range from 4 to 9, with a constant level of activity at pH 5 and above
4 - 9
activity range, pH profiles of recombinant wild-type and K42 mutant enzymes, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
UniProt
brenda
enzyme additionally catalyzes the rearrangement of chorismate into prephenate
-
-
brenda
enzyme possesses isochorismate pyruvate lyase and weak chorismate mutase activity
-
-
brenda
isochorismate-pyruvate lyase with additional chorismate mutase activity
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
highest production of isochorismate and salicylic acid in vitro by protein extracts of the young leaves of constitutively salicylic acid producing tobacco plants. Synthesis varies among the tested lines and within one line
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
evolution
-
PchB is a structural homologue of the AroQ chorismate mutases
metabolism
physiological function
additional information
-
structure-function relationship, biocatalysis of pericyclic reactions, overview. For PchB, the pericyclic reaction is a concerted but asynchronous [1,5]-sigmatropic shift with a quantitative transfer of hydrogen from C2 to C9. Major structural difference between the apo form and the pyruvate-bound or the pyruvate-and salicylate-bound forms of PchB: the active site loop between helix 1 and helix 2 is disordered in the apo structure but fully ordered in the ligand-bound structures. The difference between the open and closed structures is due to a conserved active site lysine 42, which hydrogen bonds to a bound pyruvate molecule. Quantum mechanical/molecular mechanical molecular dynamics simulations, overview
metabolism
-
the enzyme is involved in siderophore pyochelin via salicylate biosynthesis
metabolism
the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). Salicylate synthase converts chorismate into salicylate through a two-step reaction
metabolism
-
the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
metabolism
-
the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
metabolism
the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
metabolism
the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
metabolism
-
the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
-
metabolism
-
the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities
-
metabolism
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). Salicylate synthase converts chorismate into salicylate through a two-step reaction
-
physiological function
involved in the biosynthesis of the siderophore yersiniabactin
physiological function
-
the enzyme physiologically catalyzes the elimination of the enolpyruvyl side chain from isochorismate to make salicylate for incorporation into the siderophore pyochelin
physiological function
the enzyme is involved in the biosynthesis of pyochelin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria
physiological function
-
the enzyme is involved in the biosynthesis of the siderophore yersiniabactin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria
physiological function
-
the enzyme is involved in the biosynthesis of the siderophore yersiniabactin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria
physiological function
the enzyme is involved in the biosynthesis of the siderophore mycobactin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria
physiological function
mycobactins are small-molecule iron chelators (siderophores) produced by Mycobacterium tuberculosis (Mtb) for iron mobilization. Siderophores are small-molecule iron chelators that scavenge iron from host tissues and uptake of heme through a specialized heme receptor followed by heme degradation to release the iron. The bifunctional salicylate synthase MbtI catalyzes the first step of mycobactin biosynthesis through the conversion of the primary metabolite chorismate into salicylic acid via isochorismate
physiological function
-
salicylic acid (SA) is an essential hormone for development and induced defense against biotrophic pathogens in plants. The formation of SA mainly derives from chorismate via isochorismate synthase (ICS, EC 5.4.4.2) and isochorismate pyruvate lyase (IPL, EC 4.2.99.21)-mediated steps in Arabidopsis thaliana
physiological function
-
the enzyme is involved in the biosynthesis of the siderophore mycobactin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria
-
physiological function
-
mycobactins are small-molecule iron chelators (siderophores) produced by Mycobacterium tuberculosis (Mtb) for iron mobilization. Siderophores are small-molecule iron chelators that scavenge iron from host tissues and uptake of heme through a specialized heme receptor followed by heme degradation to release the iron. The bifunctional salicylate synthase MbtI catalyzes the first step of mycobactin biosynthesis through the conversion of the primary metabolite chorismate into salicylic acid via isochorismate
-
physiological function
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
the enzyme is involved in the biosynthesis of pyochelin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria
-
physiological function
Arabidopsis thaliana ecotype Di-17
-
salicylic acid (SA) is an essential hormone for development and induced defense against biotrophic pathogens in plants. The formation of SA mainly derives from chorismate via isochorismate synthase (ICS, EC 5.4.4.2) and isochorismate pyruvate lyase (IPL, EC 4.2.99.21)-mediated steps in Arabidopsis thaliana
-
Show AA Sequence and Transmembrane Helices (130 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
-
enzyme is an intertwined dimer of three helices with connecting loops, and amino acids from each monomer participate in each of two active sites, crystallization data
?
Arabidopsis thaliana ecotype Di-17
-
x * 38000, recombinant His-tagged PRXR1, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
docking studies of inhibitors (E)-3-(1-carboxyprop-1-enyloxy)-2-hydroxybenzoic acid, 3-(1-carboxy-3-methylbut-1-enyloxy)-2-hydroxybenzoic acid, 3-(1-carboxybut-1-enyloxy)-2-hydroxybenzoic acid, and 3-(1-carboxy-2-phenylvinyloxy)-2-hydroxybenzoic acid
-
native protein and selenomethionine-derivative, to 2.5-3.2 A resolution
-
apo-structure, to 2.35 A resolution, has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure, to 1.95 A resolution, has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis
-
molecular dynamics simulations and averaged intermolecular substrate-protein distances, active-site volumes for reactants and transition state
-
purified recombinant His-tagged wild-type enzyme and mutant K42E in complex with salicylate and pyruvate, hanging drop vapor diffusion method, mixing of 0.001 ml of 64 mg/ml wild-type protein with 0.001 ml of reservoir solution containing 0.2 M lithium sulfate, 0.1 M sodium acetate, pH 4.5, and 6% glycerol, mixing of 0.001 ml of 34 mg/ml mutant protein with 0.001 ml reservoir solution containing 0.004 M Gly-Gly, 0.100 M sodium acetate, pH 3.6, and 12% glycerol, ligands in 20fold molar excess, 25°C, 24-48 h, X-ray diffraction structure determination and analysis, modeling
wild-type and mutant K42E, to 1.95 and 1.79 A resolution, respectively, in complex with salicylate and pyruvate
X-ray crystallographic structures for mutant K42A with salicylate and pyruvate bound, to 2.5 A resolution, and for apo-I87T, to 2.15 A resolution. Circular dichroism studies of mutants K42A, K42Q, K42E, and K42H, A43P and I87T
-
crystal structure of Irp9 and of its complex with the reaction products salicylate and pyruvate at 1.85 A and 2.1 A resolution, respectively. Irp9 has a complex alpha/beta fold. The crystal structure of Irp9 contains one molecule each of phosphate and acetate derived from the crystallization buffer. The enzyme is still catalytically active in the crystal. Both structures contain Mg2+ in the active site. There is no evidence of an allosteric tryptophan binding site
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K147Q
-
mutation in proposed catalytic base, about 50fold decrease in activity
A375T
-
loss of the physiological isochorismate synthase catalytic efficiency by three orders of magnitude, and a 2fold gain in isochorismate-pyruvate lyase catalytic efficiency
A37I
-
mutation increases the rate constant for the chorismate mutase activity by a factor of 1000, and also increases the isochorismate pyruvate lyase catalytic efficiency, by a factor of 6
A43P
-
about 25% decrease in both chorismate mutase and isochorismate pyruvate lyase activity
C7A
-
mutant has a reduced catalytic free energy of activation of up to 0.17 kcal/mol
C7A/K42C
-
mutant has a reduced catalytic free energy of activation of up to 4.2 kcal/mol. Treatment with bromoethylamine leads to 64% recovery of activity
D310E
-
physiological isochorismate synthase catalytic efficiency similar to wild-type, 3fold gain in isochorismate-pyruvate lyase catalytic efficiency
D310E/A375T
-
similar activity in the isochorismate synthase and isochorismate-pyruvate lyase assays as the A375T variant
I87T
-
structure demonstrates considerable mobility, decrease in both chorismate mutase and isochorismate pyruvate lyase activity
I88T
-
no isochorismate pyruvate lyase activity, retains chorismate mutase activity
K42A
K42C
-
mutant has a reduced catalytic free energy of activation of up to 4.4 kcal/mol. Treatment with bromoethylamine leads to 55% recovery of activity
K42E
K42H
Q91N
-
20fold decrease in both isochorismate pyruvate lyase and chorismate mutase activity
R54K
-
100fold decrease in both isochorismate pyruvate lyase and chorismate mutase activity
D310E/A375T
more than additive effect of the two individual variants with isochorismate-pyruvate lyase catalytic efficiency three orders of magnitude less than wild-type and undetectable salicylate synthase activity
E281D
salicylate synthase catalytic efficiency is 32fold less than that of the wildtype enzyme. Isochorismate-pyruvate lyase catalytic efficiency loss of 5fold relative to the wildtype
T348A
reduction in salicylate synthase catalytic efficiency by five orders of magnitude. Isochorismate-pyruvate lyase catalytic efficiency is reduced by 17fold
D310E/A375T
-
more than additive effect of the two individual variants with isochorismate-pyruvate lyase catalytic efficiency three orders of magnitude less than wild-type and undetectable salicylate synthase activity
-
E281D
-
salicylate synthase catalytic efficiency is 32fold less than that of the wildtype enzyme. Isochorismate-pyruvate lyase catalytic efficiency loss of 5fold relative to the wildtype
-
T348A
-
reduction in salicylate synthase catalytic efficiency by five orders of magnitude. Isochorismate-pyruvate lyase catalytic efficiency is reduced by 17fold
-
additional information
K42A
-
residue presumably involved in electrostatic transition state stabilization. Active site architecture is maintained in mutant K42A
K42A
similar to wild-type, active across the entire pH-range from 4 to 9, with a constant level of activity at pH 5 and above
K42A
-
mutation leads to the recovery in catalytic free energy of activation of 2.52.7 kcal/mol compared to mutant K42C. Exogenous addition of ethylamine to the K42A variant leads to a neglible recovery of activity, whereas addition of propylamine causes an additional modest loss in catalytic power
K42E
site-directed mutagenesis of the catalytic residue, inactive mutant, crystal structure determination and comparison to the wild-type structure
K42H
the enzyme develops a pH dependence corresponding to a loss of catalytic power upon deprotonation of the histidine. With loss of the positive charge on the K42H side chain at high pH, the enzyme retains lyase activity at about 100fold lowered catalytic efficiency but loses detectable chorismate mutase activity
K42H
site-directed mutagenesis of the catalytic residue, the mutant enzyme shows 100fold lowered isochorismate lyase catalytic efficiency compared to the wild-type, but loses detectable mutase activity. It develops a pH-dependence corresponding to a loss of catalytic power upon deprotonation of the histidine. The change is not due to changes in active site architecture, but due to the difference in charge at this key site
additional information
-
development of an Escherichia coli salicylate (SA) biosensor to screen for IPL activity based on the SalR regulator/psalA promoter combination from Acinetobacter sp. ADP1, to control the expression of the reporter luxCDABE. The sensing components, including the SA-inducible promoter PsalA, the reporter operon luxCDABE and the salR gene encoding the LysR-type regulator of salA, are subcloned from Acinetobacter ADPWH_lux into a plasmid vector. The biosensor is responsive to micromolar concentrations of exogenous SA, and to endogenous SA produced after transformation with a plasmid permitting IPTG-inducible expression of bacterial IPL in this biosensor strain. After screening a cDNA library constructed from turnip crinkle virus (TCV)-infected Arabidopsis thaliana ecotype Di-17, an enzyme, PRXR1, is identified as a putative IPL that converts isochorismate into SA
additional information
Arabidopsis thaliana ecotype Di-17
-
development of an Escherichia coli salicylate (SA) biosensor to screen for IPL activity based on the SalR regulator/psalA promoter combination from Acinetobacter sp. ADP1, to control the expression of the reporter luxCDABE. The sensing components, including the SA-inducible promoter PsalA, the reporter operon luxCDABE and the salR gene encoding the LysR-type regulator of salA, are subcloned from Acinetobacter ADPWH_lux into a plasmid vector. The biosensor is responsive to micromolar concentrations of exogenous SA, and to endogenous SA produced after transformation with a plasmid permitting IPTG-inducible expression of bacterial IPL in this biosensor strain. After screening a cDNA library constructed from turnip crinkle virus (TCV)-infected Arabidopsis thaliana ecotype Di-17, an enzyme, PRXR1, is identified as a putative IPL that converts isochorismate into SA
-
additional information
-
a CM-deficient Escherichia coli mutant, which is auxotrophic for phenylalanine and tyrosine, is functionally complemented by the cloned pchB gene for growth in minimal medium
additional information
-
enzyme is not able to complement Escherichia coli entC for the production of enterobactin. Expression of Irp9 in Escherichia coli entC mutant leads to salicylate synthesis
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged PRXR1 protein from Escherichia coli by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of a fusion of genes pchA and pchB from Pseudomonas aeruginosa, which encode isochorismate synthase and isochorismate pyruvate-lyase, in Arabidopsis thaliana
-
gene prxr1, Arabidopsis thaliana cDNA library screening using XL1-LUX, recombinant expression of His-tagged PRXR1 protein in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an entB mutant of Escherichia coli blocked in the conversion of isochorismate to 2,3-dihydro-2,3-dihydroxybenzoate forms salicylate when transformed with a pchB expression construct. Salicylate formation occurs in vitro when chorismate is incubated with a crude extract of Pseudomons aeruginosa containing overproduced PchA and PchB proteins, salicylate and pyruvate are formed in equimolar amounts
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
expression of a fusion of genes pchA and pchB from Pseudomonas aeruginosa, which encode isochorismate synthase and isochorismate pyruvate-lyase, in Arabidopsis thaliana, with targeting of the gene product either to the cytosol, c-SAS plants, or to the chloroplast, p-SAS plants. In p-SAS plants, the amount of free and conjugated SA is increased more than 20fold above wild type level. P-SAS plants show a strongly dwarfed phenotype and produce very few seeds. Targeting of SAS to the cytosol causes a slight increase in free salicylic acid and a significant threefold increase in conjugated salicylic acid. The modest increase in total salicylic content does not strongly induce the resistance marker PR-1, but results in enhanced disease resistance towards a virulent isolate of Peronospora parasitica. Increased resistance of c-SAS lines is paralleled with reduced seed production
biotechnology
-
alternative computational rational approach to improve the secondary catalytic activity of enzymes, taking as a test case the IPL enzyme. The approach is based on the use of molecular dynamic simulations employing hybrid quantum mechanics/molecular mechanics methods that allow describing breaking and forming bonds
drug development
synthesis
-
alternative computational rational approach to improve the secondary catalytic activity of enzymes, taking as a test case the IPL enzyme. The approach is based on the use of molecular dynamic simulations employing hybrid quantum mechanics/molecular mechanics methods that allow describing breaking and forming bonds
drug development
enzyme MbtI represents an appealing target for development of inhibitors of mycobactin biosynthesis since it is structurally and biochemically characterized, has no human orthologues, and is conditionally essential under iron-deficient conditions. Inhibitors are designed against the isochorismatase activity of the enzyme (EC 5.4.4.2)
drug development
-
enzyme MbtI represents an appealing target for development of inhibitors of mycobactin biosynthesis since it is structurally and biochemically characterized, has no human orthologues, and is conditionally essential under iron-deficient conditions. Inhibitors are designed against the isochorismatase activity of the enzyme (EC 5.4.4.2)
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kunzler, D.E.; Sasso, S.; Gamper, M.; Hilvert, D.; Kast, P.
Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from combinatorial mutagenesis and selection
J. Biol. Chem.
280
32827-32834
2005
Pseudomonas aeruginosa
brenda
Ziebart, K.T.; Toney, M.D.
Nucleophile specificity in anthranilate synthase, aminodeoxychorismate synthase, isochorismate synthase, and salicylate synthase
Biochemistry
49
2851-2859
2010
Escherichia coli
brenda
Parsons, J.F.; Shi, K.; Calabrese, K.; Ladner, J.E.
Crystallization and x-ray diffraction analysis of salicylate synthase, a chorismate-utilizing enzyme involved in siderophore biosynthesis
Acta Crystallogr. Sect. F
F62
271-274
2006
Escherichia coli
-
brenda
Zwahlen, J.; Kolappan, S.; Zhou, R.; Kisker, C.; Tonge, P.J.
Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis
Biochemistry
46
954-964
2007
Mycobacterium tuberculosis
brenda
Luo, Q.; Olucha, J.; Lamb, A.L.
Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme
Biochemistry
48
5239-5245
2009
Pseudomonas aeruginosa
brenda
Manos-Turvey, A.; Bulloch, E.M.M.; Rutledge, P.J.; Baker, E.N.; Lott, J.S.; Payne, R.J.
Inhibition studies of Mycobacterium tuberculosis salicylate synthase (MbtI)
ChemMedChem
5
1067-1079
2010
Mycobacterium tuberculosis
brenda
DeClue, M.S.; Baldridge, K.K.; Kunzler, D.E.; Kast, P.; Hilvert, D.
Isochorismate pyruvate lyase: a pericyclic reaction mechanism?
J. Am. Chem. Soc.
127
15002-15003
2005
Pseudomonas aeruginosa
brenda
Marti, S.; Andres, J.; Moliner, V.; Silla, E.; Tunon, I.; Bertran, J.
Predicting an improvement of secondary catalytic activity of promiscuous isochorismate pyruvate lyase by computational design
J. Am. Chem. Soc.
130
2894-2895
2008
Pseudomonas aeruginosa
brenda
Marti, S.; Andres, J.; Moliner, V.; Silla, E.; Tunon, I.; Bertran, J.
Mechanism and plasticity of isochorismate pyruvate lyase: a computational study
J. Am. Chem. Soc.
131
16156-16161
2009
Pseudomonas aeruginosa
brenda
Pelludat, C.; Brem, D.; Heesemann, J.
Irp9, encoded by the high-pathogenicity island of Yersinia enterocolitica, is able to convert chorismate into salicylate, the precursor of the siderophore yersiniabactin
J. Bacteriol.
185
5648-5653
2003
Yersinia enterocolitica
brenda
Kerbarh, O.; Ciulli, A.; Howard, N.I.; Abell, C.
Salicylate biosynthesis: overexpression, purification, and characterization of Irp9, a bifunctional salicylate synthase from Yersinia enterocolitica
J. Bacteriol.
187
5061-5066
2005
Yersinia enterocolitica (Q9X9I8), Yersinia enterocolitica
brenda
Gaille, C.; Kast, P.; Haas, D.
Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities
J. Biol. Chem.
277
21768-21775
2002
Pseudomonas aeruginosa
brenda
Zaitseva, J.; Lu, J.; Olechoski, K.L.; Lamb, A.L.
Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa
J. Biol. Chem.
281
33441-33449
2006
Pseudomonas aeruginosa
brenda
Kerbarh, O.; Chirgadze, D.Y.; Blundell, T.L.; Abell, C.
Crystal structures of Yersinia enterocolitica salicylate synthase and its complex with the reaction products salicylate and pyruvate
J. Mol. Biol.
357
524-534
2006
Yersinia enterocolitica (Q9X9I8)
brenda
Serino, L.; Reimmann, C.; Baur, H.; Beyeler, M.; Visca, P.; Haas, D.
Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa
Mol. Gen. Genet.
249
217-228
1995
Pseudomonas aeruginosa (Q51507)
brenda
Payne, R.J.; Kerbarh, O.; Miguel, R.N.; Abell, A.D.; Abell, C.
Inhibition studies on salicylate synthase
Org. Biomol. Chem.
3
1825-1827
2005
Yersinia enterocolitica
brenda
Mauch, F.; Mauch-Mani, B.; Gaille, C.; Kull, B.; Haas, D.; Reimmann, C.
Manipulation of salicylate content in Arabidopsis thaliana by the expression of an engineered bacterial salicylate synthase
Plant J.
25
67-77
2001
Pseudomonas aeruginosa
brenda
Nugroho, L.H.; Verberne, M.C.; Verpoorte, R.
Salicylic acid produced by isochorismate synthase and isochorismate pyruvate lyase in various parts of constitutive salicylic acid producing tobacco plants
Plant Sci.
161
911-915
2001
Nicotiana tabacum
-
brenda
Olucha, J.; Ouellette, A.N.; Luo, Q.; Lamb, A.L.
pH Dependence of catalysis by Pseudomonas aeruginosa isochorismate-pyruvate lyase: implications for transition state stabilization and the role of lysine 42
Biochemistry
50
7198-7207
2011
Pseudomonas aeruginosa (Q51507), Pseudomonas aeruginosa
brenda
Luo, Q.; Meneely, K.M.; Lamb, A.L.
Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB
J. Am. Chem. Soc.
133
7229-7233
2011
Pseudomonas aeruginosa
brenda
Lamb, A.L.
Pericyclic reactions catalyzed by chorismate-utilizing enzymes
Biochemistry
50
7476-7483
2011
Pseudomonas aeruginosa
brenda
Choutko, A.; Eichenberger, A.P.; van Gunsteren, W.F.; Dolenc, J.
Exploration of swapping enzymatic function between two proteins: a simulation study of chorismate mutase and isochorismate pyruvate lyase
Protein Sci.
22
809-822
2013
Pseudomonas aeruginosa
brenda
Meneely, K.M.; Luo, Q.; Lamb, A.L.
Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities
Arch. Biochem. Biophys.
539
70-80
2013
Pseudomonas aeruginosa, Yersinia enterocolitica (Q9X9I8), Yersinia enterocolitica ATCC 33114 (Q9X9I8)
brenda
Olucha, J.; Meneely, K.M.; Lamb, A.L.
Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB
Biochemistry
51
7525-7532
2012
Pseudomonas aeruginosa
brenda
Svarcova, M.; Kratky, M.; Vinsova, J.
Investigation of potential inhibitors of chorismate-utilizing enzymes
Curr. Med. Chem.
22
1383-1399
2015
Mycobacterium tuberculosis (P9WFX1), Mycobacterium tuberculosis ATCC 25618 (P9WFX1), no activity in Homo sapiens, Pseudomonas aeruginosa (Q51507), Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q51507), Yersinia enterocolitica, Yersinia pestis
brenda
Liu, Z.; Liu, F.; Aldrich, C.C.
Stereocontrolled synthesis of a potential transition-state inhibitor of the salicylate synthase MbtI from Mycobacterium tuberculosis
J. Org. Chem.
80
6545-6552
2015
Mycobacterium tuberculosis (P9WFX1), Mycobacterium tuberculosis ATCC 25618 (P9WFX1)
brenda
Zhou, Y.; Memelink, J.; Linthorst, H.J.M.
An E. coli biosensor for screening of cDNA libraries for isochorismate pyruvate lyase-encoding cDNAs
Mol. Genet. Genomics
293
1181-1190
2018
Arabidopsis thaliana, Arabidopsis thaliana ecotype Di-17
brenda
Xie, L.; Yang, M.; Chen, Z.
Understanding the entropic effect in chorismate mutase reaction catalyzed by isochorismate-pyruvate lyase from Pseudomonas aeruginosa (PchB)
Catal. Sci. Technol.
9
957-965
2019
Pseudomonas aeruginosa
-
brenda
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