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acetyl coenzyme a and carboxymethyl-coenzyme a

acetyl coenzyme a has been researched along with carboxymethyl-coenzyme a in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (100.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Crane, BR; Donald, LJ; Drysdale, GR; Duckworth, HW; Kurz, LC; Shah, S1
Drysdale, GR; Evans, CT; Kurz, LC; Riley, MC; Srere, PA1
Drysdale, GR; Hsu, F; Kurz, LC; Nakra, T; Plungkhen, W; Riley, M; Stein, R1

Other Studies

3 other study(ies) available for acetyl coenzyme a and carboxymethyl-coenzyme a

ArticleYear
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 reaction.
    Biochemistry, 1992, Sep-01, Volume: 31, Issue:34

    Topics: Acetyl Coenzyme A; Acyl Coenzyme A; Allosteric Regulation; Animals; Circular Dichroism; Citrate (si)-Synthase; Escherichia coli; Hydrogen-Ion Concentration; Isoelectric Point; Magnetic Resonance Spectroscopy; Myocardium; Oxaloacetates; Potassium Chloride; Protons; Swine

1992
Catalytic strategy of citrate synthase: effects of amino acid changes in the acetyl-CoA binding site on transition-state analog inhibitor complexes.
    Biochemistry, 1992, Sep-01, Volume: 31, Issue:34

    Topics: Acetyl Coenzyme A; Acyl Coenzyme A; Animals; Aspartic Acid; Binding Sites; Catalysis; Citrate (si)-Synthase; Glycine; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Isoelectric Focusing; Isoelectric Point; Magnetic Resonance Spectroscopy; Mutagenesis; Myocardium; Oxaloacetates; Protons; Swine

1992
Effects of changes in three catalytic residues on the relative stabilities of some of the intermediates and transition states in the citrate synthase reaction.
    Biochemistry, 1998, Jul-07, Volume: 37, Issue:27

    Topics: Acetyl Coenzyme A; Acyl Coenzyme A; Amino Acid Substitution; Animals; Arginine; Asparagine; Binding Sites; Catalysis; Circular Dichroism; Citrate (si)-Synthase; Citric Acid; Enzyme Stability; Glutamine; Glycine; Histidine; Hydrolysis; Kinetics; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Oxaloacetates; Protons; Solvents; Substrate Specificity; Swine

1998