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Information on EC 4.2.99.21 - isochorismate lyase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q51507
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4.2.99.21 isochorismate lyaseIUBMB 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.
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Word Map
- 4.2.99.21
-
siderophore
-
pericyclic
-
chorismate-utilizing
- prephenate
- 2,3-dihydroxybenzoate
- anthranilate
-
mg2+-dependent
- enterobactin
- drug development
- agriculture
- biotechnology
- synthesis
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
isochorismate pyruvate lyase, isochorismate-pyruvate lyase, isochorismate lyase, prxr1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
pyochelin biosynthetic protein PchB
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-
-
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isochorismate pyruvate lyase
salicylate biosynthesis protein pchB
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-
-
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isochorismate pyruvate lyase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
[1,5]-sigmatropic reaction mechanism that invokes electrostatic catalysis in analogy to the [3,3]-pericyclic rearrangement of chorismate in chorismate mutase
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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)
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isochorismate = salicylate + pyruvate
kinetic mechanism and transition state of the elimination reaction, overview
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isochorismate = salicylate + pyruvate
reaction mechanism with catalytic residue Lys42, modeling, overview
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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
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isochorismate = salicylate + pyruvate
the lysine42 residue is required in a specific conformation to stabilize the transition state
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY
383896-77-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
isochorismate
salicylate + pyruvate
elimination of pyruvate
-
-
?
isochorismate
salicylate + pyruvate
-
-
-
-
?
isochorismate
salicylate + pyruvate
-
isochorismate undergoes elimination to form salicylate and pyruvate and rearrangement to form isoprephenate in the absence of enzyme
-
-
?
isochorismate
salicylate + pyruvate
-
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
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-
?
additional information
?
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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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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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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
-
-
?
additional information
?
-
-
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
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-
?
additional information
?
-
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PchB can also perform a nonphysiological role as a chorismate mutase, EC 4.1.3.40, albeit with considerably lower catalytic efficiency
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-
?
additional information
?
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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
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-
?
additional information
?
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isochorismate synthase PhA additionally shows isochorismate lyase activity. Site-specific mutation of active site residues promotes lyase activity
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
inhibition of salicylate synthase activity
additional information
-
not inhibitory at 1 mM: EDTA, EGTA, or o-phenanthroline. No substrate inhibition up to 1.2 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics and thermodynamics, overview
-
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
0.048
isochorismate
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mutant K42A, presence of propylamine, pH 8.0, 20°C
0.06
isochorismate
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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
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mutant K42C, treatment with bromoethanol, pH 8.0, 20°C
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
0.0128
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
0.083
isochorismate
-
mutant K42A, presence of ethylamine, pH 8.0, 20°C
0.0945
isochorismate
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mutant K42C, treatment with bromoethylamine, pH 8.0, 20°C
0.098
isochorismate
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mutant K42A, presence of propylamine, pH 8.0, 20°C
0.105
isochorismate
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mutant C7A/K42C, treatment with bromoethylamine, pH 8.0, 20°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
isochorismate
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wild-type, 25°C, pH not specified in the publication
0.0366
isochorismate
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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
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mutant C7A/K42C, treatment with bromoethanol, pH 8.0, 20°C
0.147
isochorismate
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mutant K42C, treatment with bromoethanol, pH 8.0, 20°C
1.37
isochorismate
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mutant K42A, presence of propylamine, pH 8.0, 20°C
2.06
isochorismate
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mutant K42A, presence of ethylamine, pH 8.0, 20°C
4.2
isochorismate
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mutant K42C, treatment with bromoethylamine, pH 8.0, 20°C
6.7
isochorismate
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mutant C7A/K42C, treatment with bromoethylamine, pH 8.0, 20°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0001
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
0.0001
5-[(2-carboxyphenyl)sulfamoyl]-2-hydroxybenzoic acid
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isochorismate-pyruvate lyase with additional chorismate mutase activity
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
evolution
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PchB is a structural homologue of the AroQ chorismate mutases
metabolism
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the enzyme is involved in siderophore pyochelin via salicylate biosynthesis
physiological function
-
the enzyme physiologically catalyzes the elimination of the enolpyruvyl side chain from isochorismate to make salicylate for incorporation into the siderophore pyochelin
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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molecular dynamics simulations and averaged intermolecular substrate-protein distances, active-site volumes for reactants and transition state
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K42A
K42E
K42H
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
Q91N
-
20fold decrease in both isochorismate pyruvate lyase and chorismate mutase activity
R54K
-
100fold decrease in both isochorismate pyruvate lyase and chorismate mutase activity
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
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
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
K42A
-
residue presumably involved in electrostatic transition state stabilization. Active site architecture is maintained in mutant K42A
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of a fusion of genes pchA and pchB from Pseudomonas aeruginosa, which encode isochorismate synthase and isochorismate pyruvate-lyase, in Arabidopsis thaliana
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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
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
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
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
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
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
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
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
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
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
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)
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
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
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
Lamb, A.L.
Pericyclic reactions catalyzed by chorismate-utilizing enzymes
Biochemistry
50
7476-7483
2011
Pseudomonas aeruginosa
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
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)
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
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
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