propionyl-coenzyme a has been researched along with adenosine monophosphate in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (25.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (75.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Escalante-Semerena, JC; Horswill, AR | 1 |
Boeke, JD; Celic, I; Cole, RN; Escalante-Semerena, JC; Starai, VJ | 1 |
Escalante-Semerena, JC; Gulick, AM; Homick, KM; Horswill, AR; Starai, VJ | 1 |
COON, MJ; FOOTE, JL; SIEGEL, L | 1 |
4 other study(ies) available for propionyl-coenzyme a and adenosine monophosphate
Article | Year |
---|---|
Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: residue Lys592 is required for propionyl-AMP synthesis.
Topics: Acyl Coenzyme A; Adenosine Monophosphate; Adenosine Triphosphate; Amino Acid Motifs; Coenzyme A Ligases; Conserved Sequence; Enzyme Inhibitors; Kinetics; Lysine; Mutagenesis, Site-Directed; Propionates; Salmonella enterica; Substrate Specificity | 2002 |
Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.
Topics: Acetate-CoA Ligase; Acetylation; Acyl Coenzyme A; Adenosine Monophosphate; Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Coenzyme A; Conserved Sequence; Enzyme Activation; Gene Expression Regulation, Bacterial; Immunoblotting; Lysine; Mass Spectrometry; NAD; Peptide Mapping; Salmonella enterica; Sirtuins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2002 |
The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A.
Topics: Acetate-CoA Ligase; Acetylation; Acyl Coenzyme A; Adenosine Monophosphate; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Binding, Competitive; Coenzyme A; Coenzyme A Ligases; Crystallization; Crystallography, X-Ray; Enzyme Inhibitors; Molecular Sequence Data; Protein Conformation; Salmonella enterica | 2003 |
THE ENZYMATIC SYNTHESIS OF PROPIONYL COENZYME A HOLOCARBOXYLASE FROM D-BIOTINYL 5'-ADENYLATE AND THE APOCARBOXYLASE.
Topics: Acyl Coenzyme A; Adenine Nucleotides; Adenosine Monophosphate; Adenosine Triphosphate; Animals; Biotin; Carbon Isotopes; Carboxy-Lyases; Chemical Phenomena; Chemistry; Chemistry Techniques, Analytical; Chromatography; Coenzymes; Liver; Magnesium; Rabbits; Radiometry; Research | 1965 |