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coenzyme a and adenosine 5'-o-(3-thiotriphosphate)

coenzyme a has been researched along with adenosine 5'-o-(3-thiotriphosphate) in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19901 (33.33)18.7374
1990's1 (33.33)18.2507
2000's1 (33.33)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Mitchell, T; Nishimura, JS1
Fontes, R; Sillero, A; Sillero, MA1
Attwood, PV; Cleland, WW; Rayment, I; Reinhardt, L; St Maurice, M; Surinya, KH; Wallace, JC1

Other Studies

3 other study(ies) available for coenzyme a and adenosine 5'-o-(3-thiotriphosphate)

ArticleYear
Adenosine 5'-O-(3-thio)triphosphate, a substrate and potent inhibitor of Escherichia coli succinyl-CoA synthetase. Additional evidence for a cooperative alternating-sites mechanism.
    The Journal of biological chemistry, 1984, Aug-10, Volume: 259, Issue:15

    Topics: Acyl Coenzyme A; Adenosine Diphosphate; Adenosine Triphosphate; Affinity Labels; Binding Sites; Binding, Competitive; Coenzyme A; Coenzyme A Ligases; Escherichia coli; Succinate-CoA Ligases; Succinates; Succinic Acid; Thionucleotides

1984
Acyl coenzyme A synthetase from Pseudomonas fragi catalyzes the synthesis of adenosine 5'-polyphosphates and dinucleoside polyphosphates.
    Journal of bacteriology, 1998, Volume: 180, Issue:12

    Topics: Adenine Nucleotides; Adenosine Triphosphate; Coenzyme A; Coenzyme A Ligases; Dinucleoside Phosphates; Fatty Acids; Hydrogen-Ion Concentration; Kinetics; Metals; Pseudomonas; Substrate Specificity

1998
Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme.
    Science (New York, N.Y.), 2007, Aug-24, Volume: 317, Issue:5841

    Topics: Adenosine Triphosphate; Allosteric Regulation; Binding Sites; Biotin; Catalytic Domain; Coenzyme A; Crystallography, X-Ray; Dimerization; Enzyme Activators; Models, Molecular; Mutation; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Pyruvate Carboxylase; Rhizobium etli

2007