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Isochorismate Pyruvate Lyase: A Pericyclic Reaction Mechanism?

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inferredcites →https://doi.org/10.1002/anie.200200534openalex-snapshot
Chemistry and Biology of Biosynthetic Diels–Alder Reactions
inferredcites →https://doi.org/10.1002/jcc.540141112openalex-snapshot
General atomic and molecular electronic structure system
inferredcites →https://doi.org/10.1002/prot.1095openalex-snapshot
The crystal structure of chorismate lyase shows a new fold and a tightly retained product
inferredcites →https://doi.org/10.1006/jmbi.1994.1462openalex-snapshot
The Monofunctional Chorismate Mutase from Bacillus subtilis
inferredcites →https://doi.org/10.1007/bf00290369openalex-snapshot
Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa
inferredcites →https://doi.org/10.1016/s0167-4838(98)00040-5openalex-snapshot
Enzymatic activity and partial purification of solanapyrone synthase: first enzyme catalyzing Diels–Alder reaction
inferredcites →https://doi.org/10.1016/s0969-2126(01)00618-9openalex-snapshot
Crystal Structure of Precorrin-8x Methyl Mutase
inferredcites →https://doi.org/10.1016/s0969-2126(97)00294-3openalex-snapshot
Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures
inferredcites →https://doi.org/10.1021/bi00683a013openalex-snapshot
Steady-state analysis of kinetic isotope effects in enzymic reactions
inferredcites →https://doi.org/10.1021/bi00683a014openalex-snapshot
Proton nuclear magnetic resonance investigations of fraying in double-stranded d-ApTpGpCpApT in aqueous solution
inferredcites →https://doi.org/10.1021/cr00105a003openalex-snapshot
Molecular studies on enzymes in chorismate metabolism and the enterobactin biosynthetic pathway
inferredcites →https://doi.org/10.1021/ja00238a030openalex-snapshot
Acyclic stereocontrol in catalyzed intramolecular Diels-Alder cyclizations leading to octahydronaphthalenecarboxaldehydes
inferredcites →https://doi.org/10.1021/ja003216+openalex-snapshot
Lovastatin Nonaketide Synthase Catalyzes an Intramolecular Diels−Alder Reaction of a Substrate Analogue
inferredcites →https://doi.org/10.1038/nature01483openalex-snapshot
Erratum: Attosecond control of electronic processes by intense light fields
inferredcites →https://doi.org/10.1073/pnas.111150298openalex-snapshot
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of ( i ) its substrates, chorismate and glutamine, and a product, glutamate, and ( ii ) its end-product inhibitor, l -tryptophan
inferredcites →https://doi.org/10.1073/pnas.90.18.8600openalex-snapshot
Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog.
inferredcites →https://doi.org/10.1074/jbc.m202410200openalex-snapshot
Salicylate Biosynthesis in Pseudomonas aeruginosa
inferredcites →https://doi.org/10.1074/jbc.m506883200openalex-snapshot
Mechanistic Insights into the Isochorismate Pyruvate Lyase Activity of the Catalytically Promiscuous PchB from Combinatorial Mutagenesis and Selection
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a022727openalex-snapshot
Three-Dimensional Structure of 4-Amino-4-Deoxychorismate Lyase from Escherichia coli
inferredcites →https://doi.org/10.1128/jb.187.15.5061-5066.2005openalex-snapshot
Salicylate Biosynthesis: Overexpression, Purification, and Characterization of Irp9, a Bifunctional Salicylate Synthase fromYersinia enterocolitica
inferredcites →https://doi.org/10.3109/10409239009090615openalex-snapshot
The Shikimate Pathway — A Metabolic Tree with Many Branche

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4668249openalex-extracted
Oxygen Functional Groups in Carbon Material Obtained from Pyrolysis of Heterocyclic Compounds with Their Decomposition Mechanism
inferred← citeshttps://doi.org/10.1002/2211-5463.12224openalex-snapshot
Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complex
inferred← citeshttps://doi.org/10.1002/9780470988800.ch8openalex-snapshot
Salicylic Acid
inferred← citeshttps://doi.org/10.1002/9781119312994.apr0249openalex-snapshot
Salicylic Acid
inferred← citeshttps://doi.org/10.1002/ange.201601056openalex-snapshot
Asymmetric Enzymatic Synthesis of Allylic Amines: A Sigmatropic Rearrangement Strategy
inferred← citeshttps://doi.org/10.1002/anie.201601056openalex-snapshot
Asymmetric Enzymatic Synthesis of Allylic Amines: A Sigmatropic Rearrangement Strategy
inferred← citeshttps://doi.org/10.1002/bio.70196openalex-snapshot
Review of Photoluminescent–Photochromic Nanocomposites Containing Immobilized Inorganic Lanthanide‐Doped Strontium Aluminate Nanoparticles
inferred← citeshttps://doi.org/10.1002/cbic.200700019openalex-snapshot
Nucleophile Selectivity of Chorismate‐Utilizing Enzymes
inferred← citeshttps://doi.org/10.1002/cmdc.201000137openalex-snapshot
Inhibition Studies of Mycobacterium tuberculosis Salicylate Synthase (MbtI)
inferred← citeshttps://doi.org/10.1002/cmdc.201000275openalex-snapshot
Inhibitors of the Salicylate Synthase (MbtI) from Mycobacterium tuberculosis Discovered by High‐Throughput Screening
inferred← citeshttps://doi.org/10.1002/ijch.202100071openalex-snapshot
Computations on Pericyclic Reactions Reveal the Richness of Ambimodal Transition States and Pericyclases
inferred← citeshttps://doi.org/10.1002/nadc.20060540105openalex-snapshot
Chemie
inferred← citeshttps://doi.org/10.1002/smll.202100621openalex-snapshot
UV Photochromism in Transition Metal Oxides and Hybrid Materials
inferred← citeshttps://doi.org/10.1007/978-3-642-36260-6_72openalex-snapshot
isochorismate lyase 4.2.99.21
inferred← citeshttps://doi.org/10.1007/s00214-010-0773-zopenalex-snapshot
Molecular mechanism of chorismate mutase activity of promiscuos MbtI
inferred← citeshttps://doi.org/10.1007/s10534-010-9399-9openalex-snapshot
Iron acquisition with the natural siderophore enantiomers pyochelin and enantio-pyochelin in Pseudomonas species
inferred← citeshttps://doi.org/10.1007/s11101-020-09689-2openalex-snapshot
Biosynthesis and metabolic actions of simple phenolic acids in plants
inferred← citeshttps://doi.org/10.1007/s12539-010-0095-9openalex-snapshot
Theoretical QM/MM studies of enzymatic pericyclic reactions
inferred← citeshttps://doi.org/10.1007/s40858-019-00287-yopenalex-snapshot
Differential expression of Isochorismate synthase in Catharanthus roseus during ‘Candidatus Liberibacter asiaticus’ infection
inferred← citeshttps://doi.org/10.1016/b978-0-12-386485-7.00003-xopenalex-snapshot
Hybrid Schemes Based on Quantum Mechanics/Molecular Mechanics Simulations
inferred← citeshttps://doi.org/10.1016/b978-0-12-409547-2.14682-7openalex-snapshot
Enzyme-Associated Pericyclic Reactions
inferred← citeshttps://doi.org/10.1016/j.abb.2013.09.007openalex-snapshot
Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities
inferred← citeshttps://doi.org/10.1016/j.bbapap.2015.05.001openalex-snapshot
Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy
inferred← citeshttps://doi.org/10.1016/j.bmc.2014.09.010openalex-snapshot
Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism
inferred← citeshttps://doi.org/10.1016/j.bmcl.2010.07.044openalex-snapshot
A stable analog of isochorismate for the study of MenD and other isochorismate-utilizing enzymes
inferred← citeshttps://doi.org/10.1016/j.bmcl.2023.129440openalex-snapshot
Enzymatic reconstitution of salicylate formation in promysalin biosynthesis
inferred← citeshttps://doi.org/10.1016/j.cartre.2024.100333openalex-snapshot
Oxygen functionalized carbon obtained from pyrolysis of heterocyclic compounds with their decomposition mechanism
inferred← citeshttps://doi.org/10.1016/j.cbpa.2011.12.017openalex-snapshot
Current developments and challenges in the search for a naturally selected Diels-Alderase
inferred← citeshttps://doi.org/10.1016/j.comptc.2024.114749openalex-snapshot
Predicting decomposition temperatures and carbonization feasibility of heterocycles with their decomposition mechanism
inferred← citeshttps://doi.org/10.1016/j.jmb.2005.12.078openalex-snapshot
Crystal Structures of Yersinia enterocolitica Salicylate Synthase and its Complex with the Reaction Products Salicylate and Pyruvate
inferred← citeshttps://doi.org/10.1016/j.sbi.2018.01.015openalex-snapshot
Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study
inferred← citeshttps://doi.org/10.1021/acs.biochem.5c00157openalex-snapshot
(Reverse) Evolution of a Promiscuous Isochorismate Pyruvate Lyase into an Efficient Chorismate Mutase
inferred← citeshttps://doi.org/10.1021/acs.biochem.7b01018openalex-snapshot
Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp
inferred← citeshttps://doi.org/10.1021/acs.joc.5b00455openalex-snapshot
Stereocontrolled Synthesis of a Potential Transition-State Inhibitor of the Salicylate Synthase MbtI from Mycobacterium tuberculosis
inferred← citeshttps://doi.org/10.1021/acs.joc.6b02801openalex-snapshot
Synthesis of Transition-State Inhibitors of Chorismate Utilizing Enzymes from Bromobenzene cis-1,2-Dihydrodiol
inferred← citeshttps://doi.org/10.1021/acs.orglett.6b01919openalex-snapshot
Does Nature Know Best? Pericyclic Reactions in the Daphniphyllum Alkaloid-Forming Cation Cascade
inferred← citeshttps://doi.org/10.1021/bi200599jopenalex-snapshot
pH Dependence of Catalysis by Pseudomonas aeruginosa Isochorismate–Pyruvate Lyase: Implications for Transition State Stabilization and the Role of Lysine 42
inferred← citeshttps://doi.org/10.1021/bi2009739openalex-snapshot
Pericyclic Reactions Catalyzed by Chorismate-Utilizing Enzymes
inferred← citeshttps://doi.org/10.1021/bi300472nopenalex-snapshot
Modification of Residue 42 of the Active Site Loop with a Lysine-Mimetic Side Chain Rescues Isochorismate-Pyruvate Lyase Activity in Pseudomonas aeruginosa PchB
inferred← citeshttps://doi.org/10.1021/bi900456eopenalex-snapshot
Structure−Function Analyses of Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa Suggest Differing Catalytic Mechanisms for the Two Pericyclic Reactions of This Bifunctional Enzyme
inferred← citeshttps://doi.org/10.1021/ja056714xopenalex-snapshot
Experimental and Computational Investigation of the Uncatalyzed Rearrangement and Elimination Reactions of Isochorismate
inferred← citeshttps://doi.org/10.1021/ja078334copenalex-snapshot
Predicting an Improvement of Secondary Catalytic Activity of Promiscuos Isochorismate Pyruvate Lyase by Computational Design
inferred← citeshttps://doi.org/10.1021/ja202091aopenalex-snapshot
Entropic and Enthalpic Components of Catalysis in the Mutase and Lyase Activities of Pseudomonas aeruginosa PchB
inferred← citeshttps://doi.org/10.1021/ja2034969openalex-snapshot
A Cope Rearrangement in the Reaction Catalyzed by Dimethylallyltryptophan Synthase?
inferred← citeshttps://doi.org/10.1021/ja905271gopenalex-snapshot
Mechanism and Plasticity of Isochorismate Pyruvate Lyase: A Computational Study
inferred← citeshttps://doi.org/10.1021/jacs.5b05559openalex-snapshot
Chorismatase Mechanisms Reveal Fundamentally Different Types of Reaction in a Single Conserved Protein Fold
inferred← citeshttps://doi.org/10.1021/jacs.9b06823openalex-snapshot
Discovering Biomolecules with Huisgenase Activity: Designed Repeat Proteins as Biocatalysts for (3 + 2) Cycloadditions
inferred← citeshttps://doi.org/10.1038/nchembio.1385openalex-snapshot
Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes
inferred← citeshttps://doi.org/10.1038/s41467-024-54437-1openalex-snapshot
Mechanistic basis for the emergence of EPS1 as a catalyst in salicylic acid biosynthesis of Brassicaceae
inferred← citeshttps://doi.org/10.1038/s41586-020-2743-5openalex-snapshot
An enzymatic Alder-ene reaction
inferred← citeshttps://doi.org/10.1038/s41589-018-0003-xopenalex-snapshot
Structural basis of the Cope rearrangement and cyclization in hapalindole biogenesis
inferred← citeshttps://doi.org/10.1038/s41598-017-05032-6openalex-snapshot
X-Ray snapshots of a pyridoxal enzyme: a catalytic mechanism involving concerted [1,5]-hydrogen sigmatropy in methionine γ-lyase
inferred← citeshttps://doi.org/10.1038/s41598-017-06278-wopenalex-snapshot
Mechanisms and Specificity of Phenazine Biosynthesis Protein PhzF
inferred← citeshttps://doi.org/10.1039/b517008gopenalex-snapshot
The enantioselective synthesis of elecanacin through an intramolecular naphthoquinone-vinyl ether photochemical cycloaddition
inferred← citeshttps://doi.org/10.1039/b518097jopenalex-snapshot
Reaction mechanisms : Part (ii) Pericyclic reactions
inferred← citeshttps://doi.org/10.1039/b617924jopenalex-snapshot
Reaction mechanisms : Part (ii) Pericyclic reactions
inferred← citeshttps://doi.org/10.1039/b809416kopenalex-snapshot
Biosynthesis of ethers: Unusual or common natural events?
inferred← citeshttps://doi.org/10.1039/b814552kopenalex-snapshot
Intramolecular cyclizations of polyketide biosynthesis: mining for a “Diels–Alderase”?
inferred← citeshttps://doi.org/10.1039/b901694eopenalex-snapshot
Synthesis and evaluation of 2,5-dihydrochorismate analogues as inhibitors of the chorismate-utilising enzymes
inferred← citeshttps://doi.org/10.1039/bk9781839165641-00658openalex-snapshot
Pericyclases in Natural Product Biosynthesis
inferred← citeshttps://doi.org/10.1039/bk9781839169502-00438openalex-snapshot
Cascades vs. Concerted Reactions
inferred← citeshttps://doi.org/10.1039/c004062bopenalex-snapshot
Inhibition of chorismate-utilising enzymes by 2-amino-4-carboxypyridine and 4-carboxypyridone and 5-carboxypyridone analogues
inferred← citeshttps://doi.org/10.1039/c1np00072aopenalex-snapshot
Aminobenzoates as building blocks for natural productassembly lines
inferred← citeshttps://doi.org/10.1039/c2cp23149bopenalex-snapshot
Understanding the different activities of highly promiscuous MbtI by computational methods
inferred← citeshttps://doi.org/10.1039/c8np00075aopenalex-snapshot
The expanding world of biosynthetic pericyclases: cooperation of experiment and theory for discovery
inferred← citeshttps://doi.org/10.1039/d0cc08078kopenalex-snapshot
Chorismate- and isochorismate converting enzymes: versatile catalysts acting on an important metabolic node
inferred← citeshttps://doi.org/10.1055/s-0041-1737456openalex-snapshot
Advancing the Logic of Polymer Synthesis via Skeletal Rearrangements
inferred← citeshttps://doi.org/10.1074/jbc.m110.183418openalex-snapshot
Ligand Binding Induces an Ammonia Channel in 2-Amino-2-desoxyisochorismate (ADIC) Synthase PhzE
inferred← citeshttps://doi.org/10.1074/jbc.m605470200openalex-snapshot
Two Crystal Structures of the Isochorismate Pyruvate Lyase from Pseudomonas aeruginosa
inferred← citeshttps://doi.org/10.1101/2021.08.21.457228openalex-snapshot
Mechanistic basis for the emergence of EPS1 as a catalyst in plant salicylic acid biosynthesis
inferred← citeshttps://doi.org/10.1128/jb.00338-06openalex-snapshot
The Structure of MbtI from Mycobacterium tuberculosis , the First Enzyme in the Biosynthesis of the Siderophore Mycobactin, Reveals It To Be a Salicylate Synthase
inferred← citeshttps://doi.org/10.1146/annurev.biophys.37.032807.125832openalex-snapshot
Protein Design by Directed Evolution
inferred← citeshttps://doi.org/10.1186/s12906-019-2428-5openalex-snapshot
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inferred← citeshttps://doi.org/10.1351/pac-con-13-02-02openalex-snapshot
Rearrangements in the mechanisms of the indole alkaloid prenyltransferases
inferred← citeshttps://doi.org/10.21577/1984-6835.20190049openalex-snapshot
Recent Advancement of the Cope Rearrangement in Organic Synthesis
inferred← citeshttps://doi.org/10.4161/psb.4.6.8392openalex-snapshot
Biosynthesis of salicylic acid in plants
inferred← citeshttps://doi.org/10.48550/arxiv.1711.01705openalex-snapshot
The Activation Entropy Change in Enzymatic Reaction Catalyzed by Isochorismate-Pyruvate Lyase of Pseudomonas Aeruginosa PchB
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