The partial substrate dethiaacetyl-coenzyme A mimics all critical carbon acid reactions in the condensation half-reaction catalyzed by Thermoplasma acidophilum citrate synthase (Q37394683)

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scientific article published on August 2009

Language	Label	Description	Also known as
English	The partial substrate dethiaacetyl-coenzyme A mimics all critical carbon acid reactions in the condensation half-reaction catalyzed by Thermoplasma acidophilum citrate synthase	scientific article published on August 2009

Statements

scholarly article

1 reference

Europe PubMed Central

20 August 2017

The partial substrate dethiaacetyl-coenzyme A mimics all critical carbon acid reactions in the condensation half-reaction catalyzed by Thermoplasma acidophilum citrate synthase (English)

1 reference

Europe PubMed Central

20 August 2017

Charles Z Constantine

2

object named as

Charles Z Constantine

1 reference

Europe PubMed Central

20 August 2017

T Joseph Kappock

4

object named as

T Joseph Kappock

1 reference

Europe PubMed Central

20 August 2017

1

object named as

Linda C Kurz

1 reference

Europe PubMed Central

20 August 2017

author name string

Hong Jiang

3

1 reference

Europe PubMed Central

20 August 2017

language of work or name

0 references

publication date

1 August 2009

1 reference

Europe PubMed Central

20 August 2017

1 reference

Europe PubMed Central

20 August 2017

48

1 reference

Europe PubMed Central

20 August 2017

33

1 reference

Europe PubMed Central

20 August 2017

7878-7891

1 reference

Europe PubMed Central

20 August 2017

Very fast prediction and rationalization of pKa values for protein-ligand complexes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Structure of a NADH-insensitive hexameric citrate synthase that resists acid inactivation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Very fast empirical prediction and rationalization of protein pKa values

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Effects of high pressure on solvent isotope effects of yeast alcohol dehydrogenase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Ability of single-site mutants of citrate synthase to catalyze proton transfer from the methyl group of dethiaacetyl-coenzyme A, a non-thioester substrate analog

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters

1 reference

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6 September 2017

A very short hydrogen bond provides only moderate stabilization of an enzyme-inhibitor complex of citrate synthase

1 reference

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6 September 2017

Evidence from Inhibitor Studies for Conformational Changes of Citrate Synthase

1 reference

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6 September 2017

Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Malate synthase: proof of a stepwise Claisen condensation using the double-isotope fractionation test

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

1.9-A structures of ternary complexes of citrate synthase with D- and L-malate: mechanistic implications

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

6 September 2017

Active site mutants of pig citrate synthase: effects of mutations on the enzyme catalytic and structural properties

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

26 June 2018

Catalytic Strategy of Citrate Synthase: Subunit Interactions Revealed as a Consequence of a Single Amino Acid Change in the Oxaloacetate Binding Site

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

26 June 2018

Equilibrium Constants of the Malate Dehydrogenase, Citrate Synthase, Citrate Lyase, and Acetyl Coenzyme A Hydrolysis Reactions under Physiological Conditions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

26 June 2018

Mechanism of interaction of citrate synthase with citryl-CoA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

26 June 2018

Mutation of essential catalytic residues in pig citrate synthase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

26 June 2018

Proton uptake accompanies formation of the ternary complex of citrate synthase, oxaloacetate, and the transition-state analog inhibitor, carboxymethyl-CoA. Evidence that a neutral enol is the activated form of acetyl-CoA in the citrate synthase reac

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

26 June 2018

Substrate-inhibition by acetyl-CoA in the condensation reaction between oxaloacetate and acetyl-CoA catalyzed by citrate synthase from pig heart

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

26 June 2018

Photophysics of tryptophan fluorescence: link with the catalytic strategy of the citrate synthase from Thermoplasma acidophilum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

2 September 2018

Kinetics and mechanism of the citrate synthase from the thermophilic archaeon Thermoplasma acidophilum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

2 September 2018

The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2765034

2 September 2018

Effects of changes in three catalytic residues on the relative stabilities of some of the intermediates and transition states in the citrate synthase reaction

1 reference

https://pubmed.ncbi.nlm.nih.gov/19645419

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Solid State NMR Studies of Hydrogen Bonding in a Citrate Synthase Inhibitor Complex†

1 reference

https://pubmed.ncbi.nlm.nih.gov/19645419

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Substrate polarization in enzyme catalysis: QM/MM analysis of the effect of oxaloacetate polarization on acetyl-CoA enolization in citrate synthase

1 reference

https://pubmed.ncbi.nlm.nih.gov/19645419

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Asymmetric Methyl Groups: Asymmetric Methyl Groups, and the Mechanism of Malate Synthase

1 reference

https://pubmed.ncbi.nlm.nih.gov/19645419

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Evidence from 13C NMR for polarization of the carbonyl of oxaloacetate in the active site of citrate synthase

1 reference

https://pubmed.ncbi.nlm.nih.gov/19645419

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Evidence from Fourier transform infrared spectroscopy for polarization of the carbonyl of oxaloacetate in the active site of citrate synthase

1 reference

https://pubmed.ncbi.nlm.nih.gov/19645419

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Catalytic strategy of citrate synthase: effects of amino acid changes in the acetyl-CoA binding site on transition-state analog inhibitor complexes

1 reference

https://pubmed.ncbi.nlm.nih.gov/19645419

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Acetyl-CoA enolization in citrate synthase: a quantum mechanical/molecular mechanical (QM/MM) study

1 reference

https://pubmed.ncbi.nlm.nih.gov/19645419

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI9006447

1 reference

Europe PubMed Central

20 August 2017

1 reference

Europe PubMed Central

20 August 2017

1 reference

Europe PubMed Central

20 August 2017

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