Research graph
References from Enzyme Catalysis: The Effective Molarity for Fragments of Enzyme-Bound Whole Substrates or Active-Site Amino Acid Side Chains. Local targets link to admitted publications; unresolved targets remain external evidence.
The nature of forces between large molecules of biological interest
10.1038/161707a0 · 1948 · External reference
Engineering Enzyme Specificity by “Substrate-Assisted Catalysis”
10.1126/science.3299704 · 1987 · External reference
Bronsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant
10.1002/pro.5560010111 · 1992 · External reference
Directed Bronsted analysis of the restoration of activity to a mutant enzyme by exogenous amines
10.1126/science.2538921 · 1989 · External reference
Modification of Residue 42 of the Active Site Loop with a Lysine-Mimetic Side Chain Rescues Isochorismate-Pyruvate Lyase Activity in Pseudomonas aeruginosa PchB
10.1021/bi300472n · 2012 · External reference
An Activator–Blocker Pair Provides a Controllable On–Off Switch for a Ketosteroid Isomerase Active Site Mutant
10.1021/jacs.7b03547 · 2017 · External reference
Mutant protein chemical rescue: From mechanisms to therapeutics
10.1016/j.jbc.2025.108417 · 2025 · External reference
Structure-reactivity relationships for β-galactosidase (Escherichia coli, lac Z). 3. Evidence that Glu-461 participates in Bronsted acid-base catalysis of β-D-galactopyranosyl group transfer
10.1021/bi961028j · 1996 · External reference
Structure-reactivity relationships for β-galactosidase (Escherichia coli, lac Z). 4. Mechanism for reaction of nucleophiles with the galactosyl-enzyme intermediates of E461G and E461Q β-galactosidases
10.1021/bi961029b · 1996 · External reference
How (and why?) to revive a dead enzyme: The power of chemical rescue
10.2174/187231308783334162 · 2008 · External reference
Evaluation of the Catalytic Contribution from a Positioned General Base in Ketosteroid Isomerase
10.1021/jacs.6b04796 · 2016 · External reference
An analysis of the substrate-induced rate effect in the phosphoglucomutase system
10.1021/bi00663a015 · 1976 · External reference
Kinetics and mechanism for enzyme-catalyzed reactions of substrate pieces
2023 · External reference
The Role of Protein Side Chains in Enzyme-Activating Conformational Changes: Lessons from Studies on Variant Enzymes
10.1021/acs.chemrev.5c00572 · 2025 · External reference
Enabling Role of Ligand-Driven Conformational Changes in Enzyme Evolution
10.1021/acs.biochem.2c00178 · 2022 · External reference
Enzyme Activation Through the Utilization of Intrinsic dianion binding energy
10.1093/protein/gzw064 · 2017 · External reference
Protein Flexibility and Stiffness Enable Efficient Enzymatic Catalysis
10.1021/jacs.8b10836 · 2019 · External reference
Specificity in transition state binding: The Pauling model revisited
10.1021/bi301491r · 2013 · External reference
Effective molarities for intramolecular reactions
10.1016/s0065-3160(08)60129-x · 1980 · External reference
A Substrate in Pieces: Allosteric Activation of Glycerol 3-Phosphate Dehydrogenase (NAD+). by Phosphite Dianion
10.1021/bi8001743 · 2008 · External reference
Activation of orotidine 5’-monophosphate decarboxylase by phosphite dianion: The whole substrate is the sum of two parts
10.1021/ja055493s · 2005 · External reference
Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion
10.1021/bi700409b · 2007 · External reference
The Activating Oxydianion Binding Domain for Enzyme-Catalyzed Proton Transfer, Hydride Transfer and Decarboxylation: Specificity and Enzyme Architecture
10.1021/ja5123842 · 2015 · External reference
Rescue of K12G mutant TIM by NH4+ and alkylammonium cations: The reaction of an enzyme in pieces
10.1021/ja106104h · 2010 · External reference
Enzyme Architecture: Self-Assembly of Enzyme and Substrate Pieces of Glycerol-3-Phosphate Dehydrogenase into a Robust Catalyst of Hydride Transfer
10.1021/jacs.6b09936 · 2016 · External reference
The Organization of Active Site Side Chains of Glycerol-3-phosphate Dehydrogenase Promotes Efficient Enzyme Catalysis and Rescue of Variant Enzymes
10.1021/acs.biochem.0c00175 · 2020 · External reference
Binding energy, specificity, and enzymic catalysis: the Circe effect
10.1002/9780470122884.ch4 · 1975 · External reference
Hydron Transfer Catalyzed by Triosephosphate Isomerase. Products of the Direct and Phosphite-Activated Isomerization of [1-13C]-Glycolaldehyde in D2O
10.1021/bi900636c · 2009 · External reference
Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase
10.1021/jacs.5b09328 · 2015 · External reference
Glycerol 3-Phosphate Dehydrogenase: Role of the Protein Conformational Change in Activation of a Readily Reversible Enzyme-Catalyzed Hydride Transfer Reaction
10.1021/acs.biochem.3c00702 · 2024 · External reference
Enzyme Architecture: Optimization of Transition State Stabilization from a Cation–Phosphodianion Pair
10.1021/jacs.5b02202 · 2015 · External reference
Orotidine 5’-monophosphate decarboxylase: Transition state stabilization from remote protein-phosphodianion interactions
10.1021/bi300585e · 2012 · External reference
An Examination of the Relationship between Active Site Loop Size and Thermodynamic Activation Parameters for Orotidine 5’-Monophosphate Decarboxylase from Mesophilic and Thermophilic Organisms
10.1021/bi901064k · 2009 · External reference
Catalysis by Orotidine 5’-Monophosphate Decarboxylase: Effect of 5-Fluoro and 4’-Substituents on the Decarboxylation of Two-Part Substrates
10.1021/bi301650d · 2013 · External reference
Role of a Guanidinium Cation–Phosphodianion Pair in Stabilizing the Vinyl Carbanion Intermediate of Orotidine 5’-Phosphate Decarboxylase-Catalyzed Reactions
10.1021/bi401117y · 2013 · External reference
Phosphodianion Activation of Enzymes for Catalysis of Central Metabolic Reactions
10.1021/jacs.0c13423 · 2021 · External reference
Adenylate Kinase-Catalyzed Reaction of AMP in Pieces: Enzyme Activation for Phosphoryl Transfer to Phosphite Dianion
10.1021/acs.biochem.1c00535 · 2021 · External reference
Adenylate Kinase-Catalyzed Reactions of AMP in Pieces: Specificity for Catalysis at the Nucleoside Activator and Dianion Catalytic Sites
10.1021/acs.biochem.2c00531 · 2022 · External reference
Activation of R235A Mutant Orotidine 5’-Monophosphate Decarboxylase by the Guanidinium Cation: Effective Molarity of the Cationic Side Chain of Arg-235
10.1021/bi902174q · 2010 · External reference
Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase for Catalysis of Hydride Transfer
10.1021/acs.biochem.7b01282 · 2018 · External reference
Human Glycerol 3-Phosphate Dehydrogenase: X-Ray Crystal Structures that Guide the Interpretation of Mutagenesis Studies
10.1021/acs.biochem.8b01103 · 2019 · External reference
Glycerol-3-Phosphate Dehydrogenase: The K120 and K204 Side Chains Define an Oxyanion Hole at the Enzyme Active Site
10.1021/acs.biochem.2c00053 · 2022 · External reference
The active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase
10.1042/bj1140019 · 1969 · External reference
The Entropy of Chelation
10.1021/j150546a024 · 1956 · External reference
Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
10.1073/pnas.68.8.1678 · 1971 · External reference
Enzyme Architecture: Deconstruction of the Enzyme-Activating Phosphodianion Interactions of Orotidine 5’-Monophosphate Decarboxylase
10.1021/ja505037v · 2014 · External reference
Linear Free Energy Relationships for Enzymatic Reactions: Fresh Insight from a Venerable Probe
10.1021/acs.accounts.1c00147 · 2021 · External reference
Orotidine 5’-Monophosphate Decarboxylase: Probing the Limits of the Possible for Enzyme Catalysis
10.1021/acs.accounts.8b00059 · 2018 · External reference
Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase
10.1021/jacs.8b00251 · 2018 · External reference
On the attribution and additivity of binding energies
10.1073/pnas.78.7.4046 · 1981 · External reference
Avidin
10.1016/s0065-3233(08)60411-8 · 1975 · External reference
The energy landscape of adenylate kinase during catalysis
10.1038/nsmb.2941 · 2015 · External reference
The effective molarity of the substrate phosphoryl group in the transition state for yeast OMP decarboxylase
10.1016/j.bioorg.2004.08.005 · 2005 · External reference
Anatomy of a proficient enzyme: the structure of orotidine 5’-monophosphate decarboxylase in the presence and absence of a potential transition state analog
10.1073/pnas.030409797 · 2000 · External reference
Mechanism of the Orotidine 5’-Monophosphate Decarboxylase-Catalyzed Reaction: Evidence for Substrate Destabilization
10.1021/bi900623r · 2009 · External reference
Glycerol 3-Phosphate Dehydrogenase Catalyzed Hydride Transfer: Enzyme Activation by Cofactor Pieces
10.1021/acs.biochem.4c00324 · 2024 · External reference
Utilization of Cofactor Binding Energy for Enzyme Catalysis: Formate Dehydrogenase-Catalyzed Reactions of the Whole NAD Cofactor and Cofactor Pieces
10.1021/acs.biochem.3c00290 · 2023 · External reference
Enzyme Architecture: Activation of Phosphite Dehydrogenase-Catalyzed Hydride Transfer by NAD+ Cofactor Fragments
10.1021/acs.biochem.5c00561 · 2025 · External reference
Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution
10.1073/pnas.0233793100 · 2003 · External reference
Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase
10.1021/bi00098a026 · 1991 · External reference
Contribution of Enzyme-Phosphoribosyl Contacts to Catalysis by Orotidine 5’-Phosphate Decarboxylase
10.1021/bi000818x · 2000 · External reference
Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence
10.1021/acs.biochem.8b00201 · 2018 · External reference
Protein dynamics and enzymatic chemical barrier passage
10.1021/jp207876k · 2011 · External reference
A Foundational Shift in Models for Enzyme Function
10.1021/jacs.5c02388 · 2025 · External reference
Binding energy, specificity, and enzymic catalysis: the Circe effect
10.1002/9780470122884.ch4 · ExternalCitation · doi-reference
Bronsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant
10.1002/pro.5560010111 · ExternalCitation · doi-reference
The effective molarity of the substrate phosphoryl group in the transition state for yeast OMP decarboxylase
10.1016/j.bioorg.2004.08.005 · ExternalCitation · doi-reference
Mutant protein chemical rescue: From mechanisms to therapeutics
10.1016/j.jbc.2025.108417 · ExternalCitation · doi-reference
Effective molarities for intramolecular reactions
10.1016/s0065-3160(08)60129-x · ExternalCitation · doi-reference
Avidin
10.1016/s0065-3233(08)60411-8 · ExternalCitation · doi-reference
Linear Free Energy Relationships for Enzymatic Reactions: Fresh Insight from a Venerable Probe
10.1021/acs.accounts.1c00147 · ExternalCitation · doi-reference
Orotidine 5’-Monophosphate Decarboxylase: Probing the Limits of the Possible for Enzyme Catalysis
10.1021/acs.accounts.8b00059 · ExternalCitation · doi-reference
The Organization of Active Site Side Chains of Glycerol-3-phosphate Dehydrogenase Promotes Efficient Enzyme Catalysis and Rescue of Variant Enzymes
10.1021/acs.biochem.0c00175 · ExternalCitation · doi-reference
Adenylate Kinase-Catalyzed Reaction of AMP in Pieces: Enzyme Activation for Phosphoryl Transfer to Phosphite Dianion
10.1021/acs.biochem.1c00535 · ExternalCitation · doi-reference
Glycerol-3-Phosphate Dehydrogenase: The K120 and K204 Side Chains Define an Oxyanion Hole at the Enzyme Active Site
10.1021/acs.biochem.2c00053 · ExternalCitation · doi-reference
Enabling Role of Ligand-Driven Conformational Changes in Enzyme Evolution
10.1021/acs.biochem.2c00178 · ExternalCitation · doi-reference
Adenylate Kinase-Catalyzed Reactions of AMP in Pieces: Specificity for Catalysis at the Nucleoside Activator and Dianion Catalytic Sites
10.1021/acs.biochem.2c00531 · ExternalCitation · doi-reference
Utilization of Cofactor Binding Energy for Enzyme Catalysis: Formate Dehydrogenase-Catalyzed Reactions of the Whole NAD Cofactor and Cofactor Pieces
10.1021/acs.biochem.3c00290 · ExternalCitation · doi-reference
Glycerol 3-Phosphate Dehydrogenase: Role of the Protein Conformational Change in Activation of a Readily Reversible Enzyme-Catalyzed Hydride Transfer Reaction
10.1021/acs.biochem.3c00702 · ExternalCitation · doi-reference
Glycerol 3-Phosphate Dehydrogenase Catalyzed Hydride Transfer: Enzyme Activation by Cofactor Pieces
10.1021/acs.biochem.4c00324 · ExternalCitation · doi-reference
Enzyme Architecture: Activation of Phosphite Dehydrogenase-Catalyzed Hydride Transfer by NAD+ Cofactor Fragments
10.1021/acs.biochem.5c00561 · ExternalCitation · doi-reference
Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase for Catalysis of Hydride Transfer
10.1021/acs.biochem.7b01282 · ExternalCitation · doi-reference
Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence
10.1021/acs.biochem.8b00201 · ExternalCitation · doi-reference
Human Glycerol 3-Phosphate Dehydrogenase: X-Ray Crystal Structures that Guide the Interpretation of Mutagenesis Studies
10.1021/acs.biochem.8b01103 · ExternalCitation · doi-reference
The Role of Protein Side Chains in Enzyme-Activating Conformational Changes: Lessons from Studies on Variant Enzymes
10.1021/acs.chemrev.5c00572 · ExternalCitation · doi-reference
Contribution of Enzyme-Phosphoribosyl Contacts to Catalysis by Orotidine 5’-Phosphate Decarboxylase
10.1021/bi000818x · ExternalCitation · doi-reference
Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase
10.1021/bi00098a026 · ExternalCitation · doi-reference
An analysis of the substrate-induced rate effect in the phosphoglucomutase system
10.1021/bi00663a015 · ExternalCitation · doi-reference
Modification of Residue 42 of the Active Site Loop with a Lysine-Mimetic Side Chain Rescues Isochorismate-Pyruvate Lyase Activity in Pseudomonas aeruginosa PchB
10.1021/bi300472n · ExternalCitation · doi-reference
Orotidine 5’-monophosphate decarboxylase: Transition state stabilization from remote protein-phosphodianion interactions
10.1021/bi300585e · ExternalCitation · doi-reference
Specificity in transition state binding: The Pauling model revisited
10.1021/bi301491r · ExternalCitation · doi-reference
Catalysis by Orotidine 5’-Monophosphate Decarboxylase: Effect of 5-Fluoro and 4’-Substituents on the Decarboxylation of Two-Part Substrates
10.1021/bi301650d · ExternalCitation · doi-reference
Role of a Guanidinium Cation–Phosphodianion Pair in Stabilizing the Vinyl Carbanion Intermediate of Orotidine 5’-Phosphate Decarboxylase-Catalyzed Reactions
10.1021/bi401117y · ExternalCitation · doi-reference
Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion
10.1021/bi700409b · ExternalCitation · doi-reference
A Substrate in Pieces: Allosteric Activation of Glycerol 3-Phosphate Dehydrogenase (NAD+). by Phosphite Dianion
10.1021/bi8001743 · ExternalCitation · doi-reference
Mechanism of the Orotidine 5’-Monophosphate Decarboxylase-Catalyzed Reaction: Evidence for Substrate Destabilization
10.1021/bi900623r · ExternalCitation · doi-reference
Hydron Transfer Catalyzed by Triosephosphate Isomerase. Products of the Direct and Phosphite-Activated Isomerization of [1-13C]-Glycolaldehyde in D2O
10.1021/bi900636c · ExternalCitation · doi-reference
An Examination of the Relationship between Active Site Loop Size and Thermodynamic Activation Parameters for Orotidine 5’-Monophosphate Decarboxylase from Mesophilic and Thermophilic Organisms
10.1021/bi901064k · ExternalCitation · doi-reference
Activation of R235A Mutant Orotidine 5’-Monophosphate Decarboxylase by the Guanidinium Cation: Effective Molarity of the Cationic Side Chain of Arg-235
10.1021/bi902174q · ExternalCitation · doi-reference
Structure-reactivity relationships for β-galactosidase (Escherichia coli, lac Z). 3. Evidence that Glu-461 participates in Bronsted acid-base catalysis of β-D-galactopyranosyl group transfer
10.1021/bi961028j · ExternalCitation · doi-reference
Structure-reactivity relationships for β-galactosidase (Escherichia coli, lac Z). 4. Mechanism for reaction of nucleophiles with the galactosyl-enzyme intermediates of E461G and E461Q β-galactosidases
10.1021/bi961029b · ExternalCitation · doi-reference
The Entropy of Chelation
10.1021/j150546a024 · ExternalCitation · doi-reference
Activation of orotidine 5’-monophosphate decarboxylase by phosphite dianion: The whole substrate is the sum of two parts
10.1021/ja055493s · ExternalCitation · doi-reference
Rescue of K12G mutant TIM by NH4+ and alkylammonium cations: The reaction of an enzyme in pieces
10.1021/ja106104h · ExternalCitation · doi-reference
Enzyme Architecture: Deconstruction of the Enzyme-Activating Phosphodianion Interactions of Orotidine 5’-Monophosphate Decarboxylase
10.1021/ja505037v · ExternalCitation · doi-reference
The Activating Oxydianion Binding Domain for Enzyme-Catalyzed Proton Transfer, Hydride Transfer and Decarboxylation: Specificity and Enzyme Architecture
10.1021/ja5123842 · ExternalCitation · doi-reference
Phosphodianion Activation of Enzymes for Catalysis of Central Metabolic Reactions
10.1021/jacs.0c13423 · ExternalCitation · doi-reference
Enzyme Architecture: Optimization of Transition State Stabilization from a Cation–Phosphodianion Pair
10.1021/jacs.5b02202 · ExternalCitation · doi-reference
Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase
10.1021/jacs.5b09328 · ExternalCitation · doi-reference
A Foundational Shift in Models for Enzyme Function
10.1021/jacs.5c02388 · ExternalCitation · doi-reference
Evaluation of the Catalytic Contribution from a Positioned General Base in Ketosteroid Isomerase
10.1021/jacs.6b04796 · ExternalCitation · doi-reference
Enzyme Architecture: Self-Assembly of Enzyme and Substrate Pieces of Glycerol-3-Phosphate Dehydrogenase into a Robust Catalyst of Hydride Transfer
10.1021/jacs.6b09936 · ExternalCitation · doi-reference
An Activator–Blocker Pair Provides a Controllable On–Off Switch for a Ketosteroid Isomerase Active Site Mutant
10.1021/jacs.7b03547 · ExternalCitation · doi-reference
Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase
10.1021/jacs.8b00251 · ExternalCitation · doi-reference
Protein Flexibility and Stiffness Enable Efficient Enzymatic Catalysis
10.1021/jacs.8b10836 · ExternalCitation · doi-reference
Protein dynamics and enzymatic chemical barrier passage
10.1021/jp207876k · ExternalCitation · doi-reference
The nature of forces between large molecules of biological interest
10.1038/161707a0 · ExternalCitation · doi-reference
The energy landscape of adenylate kinase during catalysis
10.1038/nsmb.2941 · ExternalCitation · doi-reference
The active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase
10.1042/bj1140019 · ExternalCitation · doi-reference
Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution
10.1073/pnas.0233793100 · ExternalCitation · doi-reference
Anatomy of a proficient enzyme: the structure of orotidine 5’-monophosphate decarboxylase in the presence and absence of a potential transition state analog
10.1073/pnas.030409797 · ExternalCitation · doi-reference
Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
10.1073/pnas.68.8.1678 · ExternalCitation · doi-reference
On the attribution and additivity of binding energies
10.1073/pnas.78.7.4046 · ExternalCitation · doi-reference
Enzyme Activation Through the Utilization of Intrinsic dianion binding energy
10.1093/protein/gzw064 · ExternalCitation · doi-reference
Directed Bronsted analysis of the restoration of activity to a mutant enzyme by exogenous amines
10.1126/science.2538921 · ExternalCitation · doi-reference
Engineering Enzyme Specificity by “Substrate-Assisted Catalysis”
10.1126/science.3299704 · ExternalCitation · doi-reference
How (and why?) to revive a dead enzyme: The power of chemical rescue
10.2174/187231308783334162 · ExternalCitation · doi-reference
