ArticleBiochemistry2011
pH Dependence of catalysis by Pseudomonas aeruginosa isochorismate-pyruvate lyase: implications for transition state stabilization and the role of lysine 42.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Chemical Synthesis and Characterization of Lanthanum(III) 2‑Hydroxybenzoate and Its Antibacterial Potential:ACS omega · 2026Article
- (Reverse) Evolution of a Promiscuous Isochorismate Pyruvate Lyase into an Efficient Chorismate Mutase.Biochemistry · 2025Article
- Accurate Computation of Thermodynamic Activation Parameters in the Chorismate Mutase Reaction from Empirical Valence Bond Simulations.Journal of chemical theory and computation · 2024Article
- Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study.Current opinion in structural biology · 2018Review
- Mechanism-based site-directed mutagenesis to shift the optimum pH of the phenylalanine ammonia-lyase fromBiotechnology reports (Amsterdam, Netherlands) · 2014Article
- Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities.Archives of biochemistry and biophysics · 2013Article
- Lysine221 is the general base residue of the isochorismate synthase from Pseudomonas aeruginosa (PchA) in a reaction that is diffusion limited.Archives of biochemistry and biophysics · 2013Article
- 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 · 2012Article
- Pericyclic reactions catalyzed by chorismate-utilizing enzymes.Biochemistry · 2011Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
An isochorismate-pyruvate lyase with adventitious chorismate mutase activity from Pseudomonas aerugionsa (PchB) achieves catalysis of both pericyclic reactions in part by the stabilization of reactive conformations and in part by electrostatic transition-state stabilization. When the active site loop Lys42 is mutated to histidine, the enzyme develops a pH dependence corresponding to a loss of catalytic power upon deprotonation of the histidine. Structural data indicate that the change is not due to changes in active site architecture, but due to the difference in charge at this key site. With loss of the positive charge on the K42H side chain at high pH, the enzyme retains lyase activity at ∼100-fold lowered catalytic efficiency but loses detectable mutase activity. We propose that both substrate organization and electrostatic transition state stabilization contribute to catalysis. However, the dominant reaction path for catalysis is dependent on reaction conditions, which influence the electrostatic properties of the enzyme active site amino acid side chains.
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