alanine has been researched along with malonyl coenzyme a in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (20.00) | 18.7374 |
| 1990's | 2 (20.00) | 18.2507 |
| 2000's | 6 (60.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Jackowski, S; Rock, CO | 1 |
| Brown, GK; Scholem, RD | 1 |
| Corkey, BE; Curtiss, D; Kilpatrick, L; Nachiappan, V | 1 |
| Arvidson, DN; Shi, J; Woldegiorgis, G; Zhu, H | 1 |
| Asins, G; Gómez-Puertas, P; Hegardt, FG; Morillas, M; Roca, R; Serra, D; Valencia, A | 1 |
| Asins, G; Bentebibel, A; Casals, N; Gómez-Puertas, P; Hegardt, FG; Morillas, M; Sellés, E; Serra, D; Valencia, A | 1 |
| Nakayama, T; Nishino, T; Suzuki, H | 1 |
| Dai, J; Haro, D; Marrero, PF; Napal, L; Treber, M; Woldegiorgis, G | 1 |
| Kelleher, NL; McLoughlin, SM; Tseng, CC; Walsh, CT | 1 |
| Dai, J; Liu, H; Treber, M; Woldegiorgis, G; Zheng, G | 1 |
10 other study(ies) available for alanine and malonyl coenzyme a
| Article | Year |
|---|---|
Consequences of reduced intracellular coenzyme A content in Escherichia coli.
Topics: Acetyl Coenzyme A; Alanine; Citric Acid Cycle; Coenzyme A; Escherichia coli; Glutathione; Malonyl Coenzyme A; Mutation; Phospholipids | 1986 |
Metabolism of malonic semialdehyde in man.
Topics: Acetyl Coenzyme A; Acyl Coenzyme A; Alanine; Carbon Dioxide; Carboxy-Lyases; Cell Line; Fibroblasts; Humans; Liver; Malonates; Malondialdehyde; Malonyl Coenzyme A; Mitochondria; Oxidation-Reduction | 1983 |
Cytokines inhibit fatty acid oxidation in isolated rat hepatocytes: synergy among TNF, IL-6, and IL-1.
Topics: Acetyl Coenzyme A; Alanine; Animals; Cells, Cultured; Citric Acid Cycle; Depression, Chemical; Drug Synergism; Energy Metabolism; Fatty Acids; Interleukin-1; Interleukin-6; Ketone Bodies; Liver; Malonyl Coenzyme A; Models, Biological; Oxidation-Reduction; Pyruvates; Pyruvic Acid; Rats; Rats, Sprague-Dawley; Tumor Necrosis Factor-alpha | 1994 |
A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA inhibition and high affinity binding.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Blotting, Western; Carnitine O-Palmitoyltransferase; Glutamic Acid; Liver; Malonyl Coenzyme A; Molecular Sequence Data; Point Mutation; Rats; Structure-Activity Relationship | 1999 |
Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT): mutation of CPT I histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity.
Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Carnitine Acyltransferases; Carnitine O-Palmitoyltransferase; Catalysis; Catalytic Domain; Dose-Response Relationship, Drug; Histidine; Kinetics; Malonyl Coenzyme A; Mice; Models, Molecular; Molecular Sequence Data; Multigene Family; Mutagenesis, Site-Directed; Mutation; Plasmids; Protein Conformation; Protein Isoforms; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Saccharomyces cerevisiae; Sequence Homology, Amino Acid | 2001 |
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition. Mutation of methionine 593 abolishes malonyl-CoA inhibition.
Topics: Alanine; Algorithms; Amino Acid Sequence; Amino Acids; Animals; Binding Sites; Blotting, Western; Carnitine Acyltransferases; Carnitine O-Palmitoyltransferase; Catalysis; Cysteine; Dose-Response Relationship, Drug; Humans; Inhibitory Concentration 50; Kinetics; Malonyl Coenzyme A; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Point Mutation; Protein Binding; Protein Isoforms; Rats; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Threonine | 2003 |
Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin 5-O-glucoside-6'''-O-malonyltransferase from flowers of Salvia splendens, a member of the versatile plant acyltransferase family.
Topics: Acyltransferases; Alanine; Amino Acid Sequence; Amino Acid Substitution; Amino Acids; Anthocyanins; Coenzyme A; Enzyme Inhibitors; Flowers; Hydrogen-Ion Concentration; Kinetics; Malonyl Coenzyme A; Molecular Sequence Data; Multigene Family; Mutagenesis, Site-Directed; Plant Proteins; Salvia; Sequence Alignment; Sequence Homology, Amino Acid | 2003 |
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme.
Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Blotting, Western; Carnitine; Carnitine O-Palmitoyltransferase; Chickens; Dose-Response Relationship, Drug; Glutamic Acid; Glutamine; Humans; Immunoblotting; Kinetics; Liver; Lysine; Malonyl Coenzyme A; Mice; Molecular Sequence Data; Muscles; Mutation; Palmitoyl Coenzyme A; Pichia; Polymerase Chain Reaction; Protein Isoforms; Protein Structure, Tertiary; Rats; Sequence Homology, Amino Acid; Swine | 2003 |
Role of the active site cysteine of DpgA, a bacterial type III polyketide synthase.
Topics: Acetyl Coenzyme A; Alanine; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Carbon Radioisotopes; Catalysis; Coenzyme A Ligases; Cysteine; Decarboxylation; Kinetics; Malonyl Coenzyme A; Molecular Sequence Data; Mutagenesis, Site-Directed; Substrate Specificity | 2004 |
Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis.
Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Blotting, Western; Carnitine; Carnitine O-Palmitoyltransferase; Catalysis; Cysteine; DNA Primers; Humans; Kinetics; Malonyl Coenzyme A; Models, Chemical; Molecular Sequence Data; Mutagenesis; Mutation; Myocardium; Palmitic Acid; Palmitoylcarnitine; Pichia; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Serine | 2005 |