lauric acid has been researched along with heme in 14 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 9 (64.29) | 18.2507 |
2000's | 3 (21.43) | 29.6817 |
2010's | 2 (14.29) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Boyle, JM; Gibson, CF; Lian, LY; Modi, S; Primrose, WU; Roberts, GC | 1 |
Bambal, RB; Hanzlik, RP | 1 |
Roberts, GC | 1 |
Feyereisen, R; Murataliev, MB | 1 |
Alterman, MA; Bambal, RB; Chaurasia, CS; Hanzlik, RP; Lu, P | 1 |
Alayrac, C; Durst, F; Helvig, C; Koop, D; Mioskowski, C; Poullain, D; Salaün, JP | 1 |
Macdonald, ID; Munro, AW; Smith, WE | 1 |
Fisher, MB; Fujii-Kuriyama, Y; Rettie, AE; Yokotani, N; Zheng, YM | 1 |
Chapman, SK; Chumanov, GD; Hanzlik, RP; Munro, AW; Noble, MA; Quaroni, L; Turner, KL | 1 |
Baer, BR; Henne, KR; Kneller, MB; Kunze, KL; Rettie, AE; Zheng, YM | 1 |
Baer, BR; Cheesman, MJ; Gillam, EM; Rettie, AE; Zheng, YM | 1 |
Feyereisen, R; Girvan, HM; Guzov, VM; Munro, AW; Murataliev, M; Noble, MA; Smith, SJ; Smith, WE | 1 |
Cheesman, MR; Fisher, K; Girvan, HM; Levy, CW; Leys, D; Munro, AW; Rigby, SE; Williams, P | 1 |
Chavez, G; Cheruzel, LE; Dao, T; Dwaraknath, S; Mahadevan, S; Mullen, S; Nguyen, A; Nguyen, D; Nguyen, TA; Tran, NH | 1 |
1 review(s) available for lauric acid and heme
Article | Year |
---|---|
The other kind of biological NMR--studies of enzyme-substrate interactions.
Topics: beta-Lactamases; Binding Sites; Chloramphenicol O-Acetyltransferase; Cytochrome P-450 Enzyme System; Enzymes; Heme; Humans; Lauric Acids; Magnetic Resonance Spectroscopy; Models, Molecular | 1996 |
13 other study(ies) available for lauric acid and heme
Article | Year |
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NMR studies of substrate binding to cytochrome P450 BM3: comparisons to cytochrome P450 cam.
Topics: Bacillus megaterium; Bacterial Proteins; Binding Sites; Camphor 5-Monooxygenase; Cytochrome P-450 Enzyme System; Electrochemistry; Heme; Iron; Lauric Acids; Magnetic Resonance Spectroscopy; Mixed Function Oxygenases; Models, Molecular; Molecular Structure; NADPH-Ferrihemoprotein Reductase; Protein Conformation; Substrate Specificity | 1995 |
Active site structure and substrate specificity of cytochrome P450 4A1: steric control of ligand approach perpendicular to heme plane.
Topics: Allosteric Regulation; Binding Sites; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme System; Dicarboxylic Acids; Fatty Acids, Monounsaturated; Fatty Acids, Unsaturated; Heme; Kinetics; Lauric Acids; Ligands; Mixed Function Oxygenases; Recombinant Fusion Proteins; Substrate Specificity | 1996 |
Functional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain.
Topics: Bacterial Proteins; Carbon Monoxide; Catalysis; Cytochrome c Group; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Electron Transport; Escherichia coli; Fatty Acids; Flavoproteins; Heme; Hydroxylation; Lauric Acids; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Binding; Spectrometry, Fluorescence | 1996 |
Heme-coordinating analogs of lauric acid as inhibitors of fatty acid omega-hydroxylation.
Topics: Animals; Clofibrate; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme Inhibitors; Enzyme Inhibitors; Heme; Lauric Acids; Microsomes, Liver; Mixed Function Oxygenases; Rats; Rats, Sprague-Dawley; Recombinant Fusion Proteins; Structure-Activity Relationship | 1997 |
Suicide inactivation of cytochrome P450 by midchain and terminal acetylenes. A mechanistic study of inactivation of a plant lauric acid omega-hydroxylase.
Topics: Acetylene; Animals; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme Inhibitors; Heme; Lauric Acids; Microsomes; Mixed Function Oxygenases; Plant Proteins; Plants; Rabbits; Structure-Activity Relationship | 1997 |
Fatty acid-induced alteration of the porphyrin macrocycle of cytochrome P450 BM3.
Topics: Bacterial Proteins; Binding Sites; Cytochrome P-450 Enzyme System; Heme; Lauric Acids; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Palmitic Acid; Protein Binding; Recombinant Proteins; Spectrophotometry; Spectrum Analysis, Raman | 1998 |
Identification of a meander region proline residue critical for heme binding to cytochrome P450: implications for the catalytic function of human CYP4B1.
Topics: Animals; Aryl Hydrocarbon Hydroxylases; Binding Sites; Catalysis; Cytochrome P-450 Enzyme System; Heme; Humans; Hydroxylation; Insecta; Lauric Acids; Mutagenesis, Site-Directed; Proline; Rabbits; Rats; Serine; Steroid Hydroxylases; Testosterone | 1998 |
Imidazolyl carboxylic acids as mechanistic probes of flavocytochrome P-450 BM3.
Topics: Arachidonic Acid; Bacterial Proteins; Binding Sites; Catalysis; Circular Dichroism; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Enzyme Inhibitors; Fatty Acids; Heme; Imidazoles; Kinetics; Lauric Acids; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Protein Structure, Tertiary; Spectrophotometry, Ultraviolet; Substrate Specificity | 1998 |
Covalent heme binding to CYP4B1 via Glu310 and a carbocation porphyrin intermediate.
Topics: Aryl Hydrocarbon Hydroxylases; Dimerization; Glutamic Acid; Heme; Lauric Acids; Mutation; Oxygen; Porphyrins | 2003 |
Rabbit CYP4B1 engineered for high-level expression in Escherichia coli: ligand stabilization and processing of the N-terminus and heme prosthetic group.
Topics: Amino Acid Sequence; Animals; Aryl Hydrocarbon Hydroxylases; Base Sequence; Benzoflavones; Biochemistry; Cell Membrane; Enzyme Stability; Escherichia coli; Gene Expression; Heme; Lauric Acids; Ligands; Mass Spectrometry; Molecular Sequence Data; Protein Engineering; Protein Processing, Post-Translational; Rabbits; Recombinant Proteins | 2003 |
Analysis of the interactions of cytochrome b5 with flavocytochrome P450 BM3 and its domains.
Topics: Animals; Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Cytochromes b5; Electron Transport; Flavin-Adenine Dinucleotide; Flavins; Heme; Houseflies; Kinetics; Lauric Acids; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Conformation; Spectrophotometry, Ultraviolet; Substrate Specificity | 2007 |
Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450 BM3: characterization of glutamate substitution mutants at the haem site of P450 BM3.
Topics: Arachidonic Acid; Bacterial Proteins; Crystallography; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Esters; Glutamic Acid; Heme; Kinetics; Lauric Acids; Mutagenesis, Site-Directed; Mutation; NADPH-Ferrihemoprotein Reductase; Potentiometry; Protein Structure, Tertiary; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Substrate Specificity | 2010 |
An efficient light-driven P450 BM3 biocatalyst.
Topics: Bacillus megaterium; Bacterial Proteins; Coordination Complexes; Cytochrome P-450 Enzyme System; Enzyme Stability; Heme; Hydroxylation; Lauric Acids; Light; Models, Molecular; NADPH-Ferrihemoprotein Reductase; Photosensitizing Agents; Ruthenium | 2013 |