nad has been researched along with crotonyl-coenzyme a in 12 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (16.67) | 18.7374 |
| 1990's | 1 (8.33) | 18.2507 |
| 2000's | 3 (25.00) | 29.6817 |
| 2010's | 4 (33.33) | 24.3611 |
| 2020's | 2 (16.67) | 2.80 |
| Authors | Studies |
|---|---|
| Hohenegger, M; Kramar, R; Kremser, K; Mayer, M | 1 |
| Schulz, H; Yang, SY | 1 |
| Aschauer, H; Bergler, H; Ebeling, A; Fuchsbichler, S; Högenauer, G; Kollenz, G; Leitinger, B; Turnowsky, F; Wallner, P | 1 |
| Dar, MJ; Kapoor, M; Surolia, A; Surolia, N | 1 |
| Ando, M; Nishihara, H; Oka, T; Toraya, T; Yamanishi, M | 1 |
| Buckel, W; Hinderberger, J; Li, F; Seedorf, H; Thauer, RK; Zhang, J | 1 |
| Huang, H; Moll, J; Thauer, RK; Wang, S | 1 |
| Guo, F; Zhu, G | 1 |
| Eggers, J; Steinbüchel, A | 1 |
| Buckel, W; Chowdhury, NP; Klomann, K; Seubert, A | 1 |
| Buckel, W; Chowdhury, N; Franz-Badur, S; Hille, R; Niks, D; Vigil, W | 1 |
| Hille, R; Nguyen, D; Niks, D; Vigil, W | 1 |
12 other study(ies) available for nad and crotonyl-coenzyme a
| Article | Year |
|---|---|
Fatty acyl-CoA oxidase in rat kidney and liver after application of thyroxine.
Topics: Acyl Coenzyme A; Acyl-CoA Oxidase; Animals; Carnitine O-Acetyltransferase; Energy Metabolism; Kidney; Liver; Male; Microbodies; NAD; Oxidoreductases; Rats; Thyroxine | 1986 |
The large subunit of the fatty acid oxidation complex from Escherichia coli is a multifunctional polypeptide. Evidence for the existence of a fatty acid oxidation operon (fad AB) in Escherichia coli.
Topics: 3-Hydroxyacyl CoA Dehydrogenases; Acetyl-CoA C-Acyltransferase; Acyl Coenzyme A; Carbon-Carbon Double Bond Isomerases; Dodecenoyl-CoA Isomerase; Enoyl-CoA Hydratase; Escherichia coli; Iodoacetamide; Isomerases; Macromolecular Substances; Multienzyme Complexes; NAD; Operon; Racemases and Epimerases | 1983 |
Protein EnvM is the NADH-dependent enoyl-ACP reductase (FabI) of Escherichia coli.
Topics: Acyl Coenzyme A; Amino Acid Sequence; Bacterial Proteins; Carrier Proteins; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); Escherichia coli; Escherichia coli Proteins; Fatty Acid Synthase, Type II; Kinetics; Molecular Sequence Data; NAD; Oxidoreductases; Pharmaceutical Preparations; Sequence Homology, Amino Acid | 1994 |
Kinetic determinants of the interaction of enoyl-ACP reductase from Plasmodium falciparum with its substrates and inhibitors.
Topics: Acyl Coenzyme A; Animals; Antimalarials; Cloning, Molecular; Drug Design; Drug Resistance; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Fatty Acid Synthase, Type II; Fatty Acid Synthases; Humans; Kinetics; Malaria, Falciparum; NAD; Oxidoreductases; Plasmodium falciparum; Recombinant Proteins; Substrate Specificity; Triclosan | 2001 |
Novel pathway for utilization of cyclopropanecarboxylate by Rhodococcus rhodochrous.
Topics: Acyl Coenzyme A; Crotonates; Culture Media; Cyclopropanes; NAD; Oxidation-Reduction; Rhodococcus | 2004 |
Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri.
Topics: Acyl Coenzyme A; Butyryl-CoA Dehydrogenase; Catalysis; Clostridium kluyveri; Electron-Transferring Flavoproteins; Ferredoxins; Hydrogen; NAD; Oxidation-Reduction | 2008 |
NADP+ reduction with reduced ferredoxin and NADP+ reduction with NADH are coupled via an electron-bifurcating enzyme complex in Clostridium kluyveri.
Topics: Acyl Coenzyme A; Bacterial Proteins; Clostridium kluyveri; Ferredoxins; NAD; NADP; Oxidation-Reduction | 2010 |
Presence and removal of a contaminating NADH oxidation activity in recombinant maltose-binding protein fusion proteins expressed in Escherichia coli.
Topics: Acyl Coenzyme A; Artifacts; Cryptosporidium parvum; Escherichia coli; Glycerol; Maltose-Binding Proteins; NAD; Octoxynol; Oxidation-Reduction; Protozoan Proteins; Recombinant Fusion Proteins | 2012 |
Poly(3-hydroxybutyrate) degradation in Ralstonia eutropha H16 is mediated stereoselectively to (S)-3-hydroxybutyryl coenzyme A (CoA) via crotonyl-CoA.
Topics: Acyl Coenzyme A; Bacterial Proteins; Carboxylic Ester Hydrolases; Chromatography, Liquid; Cupriavidus necator; DNA-Binding Proteins; Escherichia coli; Gene Deletion; Hydroxybutyrates; Mass Spectrometry; Metabolic Engineering; Metabolic Networks and Pathways; NAD; Polyesters | 2013 |
Reduction of Flavodoxin by Electron Bifurcation and Sodium Ion-dependent Reoxidation by NAD+ Catalyzed by Ferredoxin-NAD+ Reductase (Rnf).
Topics: Acidaminococcus; Acyl Coenzyme A; Bacterial Proteins; Benzoquinones; Butyryl-CoA Dehydrogenase; Catalysis; Electron Transport; Electron-Transferring Flavoproteins; Electrons; Hydrogen; Hydroquinones; Kinetics; NAD; Oxidation-Reduction; Oxidoreductases; Recombinant Proteins; Riboflavin; Sodium; Spectrophotometry | 2016 |
Spectral deconvolution of redox species in the crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase from Megasphaera elsdenii. A flavin-dependent bifurcating enzyme.
Topics: Acyl Coenzyme A; Bacterial Proteins; Megasphaera elsdenii; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction | 2021 |
Rapid-reaction kinetics of the butyryl-CoA dehydrogenase component of the electron-bifurcating crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase from Megasphaera elsdenii.
Topics: Butyryl-CoA Dehydrogenase; Electron Spin Resonance Spectroscopy; Electrons; Ferredoxins; Kinetics; Megasphaera elsdenii; Models, Molecular; NAD; Oxidation-Reduction; Oxidoreductases; Protein Structure, Tertiary | 2023 |