coenzyme a has been researched along with adenosine 5'-o-(3-thiotriphosphate) in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (33.33) | 18.7374 |
1990's | 1 (33.33) | 18.2507 |
2000's | 1 (33.33) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Mitchell, T; Nishimura, JS | 1 |
Fontes, R; Sillero, A; Sillero, MA | 1 |
Attwood, PV; Cleland, WW; Rayment, I; Reinhardt, L; St Maurice, M; Surinya, KH; Wallace, JC | 1 |
3 other study(ies) available for coenzyme a and adenosine 5'-o-(3-thiotriphosphate)
Article | Year |
---|---|
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.
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.
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.
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 |