proline has been researched along with flavin-adenine dinucleotide in 33 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 5 (15.15) | 18.7374 |
| 1990's | 10 (30.30) | 18.2507 |
| 2000's | 12 (36.36) | 29.6817 |
| 2010's | 5 (15.15) | 24.3611 |
| 2020's | 1 (3.03) | 2.80 |
| Authors | Studies |
|---|---|
| Cecchini, G; Kearney, EB; Lipsick, J; Perl, M; Singer, TP | 1 |
| Scarpulla, RC; Soffer, RL | 1 |
| Jaenicke, R; Risse, B; Rudolph, R; Schumacher, G; Stempfer, G | 1 |
| Miura, R; Miyake, Y | 1 |
| Abeles, RH; Schonbrunn, A; Walsh, CT | 1 |
| Miura, R; Miyake, Y; Nishina, Y; Ohta, M; Shiga, K; Tojo, H; Watari, H; Yamano, T | 1 |
| Fisher, M; Harbron, S; Rabin, BR | 1 |
| Hachtel, W; Schöndorf, T | 1 |
| Brown, ED; Wood, JM | 1 |
| Dodt, G; Karl, C; Mihalik, SJ; Reimann, SA; Reuber, BE | 1 |
| Maloy, S; Muro-Pastor, AM; Ostrovsky, P | 1 |
| Andreesen, JR; Becker, D; Schräder, T | 1 |
| Diekmann, H; Ghisla, S; Macheroux, P; Seth, O; Singh, M; Smau, L; Stehr, M | 1 |
| Jorns, MS; Mathews, FS; Trickey, P; Wagner, MA | 1 |
| Maloy, S; Surber, MW | 1 |
| Becker, DF; Docherty, P; Gincherman, Y; Spilling, CD; Zhu, W | 1 |
| Bell, AF; Luo, L; Stankovich, MT; Stephens, AW; Tonge, PJ; Wu, J | 1 |
| Barber, MJ; Bewley, MC; Davis, CA; Marohnic, CC; Taormina, D | 1 |
| Baban, BA; Becker, DF; Schuermann, JP; Tanner, JJ; White, TA; Zhang, M | 1 |
| Becker, DF; Zhang, W; Zhou, Y | 1 |
| Chebotareva, NA; Harding, SE; Kurganov, BI; Winzor, DJ | 1 |
| Almashanu, S; Bender, HU; Hu, CA; Lin, WW; Pulver, A; Steel, G; Valle, D; Willis, A | 1 |
| Barber, MJ; Crowley, LJ; Davis, CA; Marohnic, CC; Smith, ET | 1 |
| Becker, DF; Krishnan, N | 1 |
| Becker, DF; Krishnan, N; Tanner, JJ; White, TA | 1 |
| Leys, D; Monaghan, PJ; Scrutton, NS | 1 |
| Atkin, KE; Bailey, KR; Brzozowski, AM; Grogan, G; Hart, S; Koehler, V; Reiss, R; Turkenburg, JP; Turner, NJ | 1 |
| Doi, K; Hara, Y; Ohshima, T; Sakuraba, H; Satomura, T; Zhang, XD | 1 |
| Becker, DF; Moxley, MA | 1 |
| Diogo de Melo, P; Elias, MC; Kowaltowski, AJ; Paes, LS; Pral, EM; Silber, AM; Suárez Mantilla, B; Tahara, EB; Zimbres, FM | 1 |
| Holmes, RP; Johnson, LC; Jönsson, TJ; Lowther, WT; Parsonage, D; Summitt, CB | 1 |
| Becker, DF; Liu, LK; Tanner, JJ | 1 |
| Yildiz, I | 1 |
1 review(s) available for proline and flavin-adenine dinucleotide
| Article | Year |
|---|---|
Structure, function, and mechanism of proline utilization A (PutA).
Topics: 1-Pyrroline-5-Carboxylate Dehydrogenase; Amino Acid Metabolism, Inborn Errors; Animals; Bacterial Proteins; Flavin-Adenine Dinucleotide; Flavoproteins; Gram-Negative Bacteria; Humans; Membrane Proteins; Proline; Proline Oxidase | 2017 |
32 other study(ies) available for proline and flavin-adenine dinucleotide
| Article | Year |
|---|---|
Transport and binding of riboflavin by Bacillus subtilis.
Topics: Bacillus subtilis; Biological Transport; Cell Membrane; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Kinetics; Phosphorylation; Proline; Riboflavin | 1979 |
Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization.
Topics: Amino Acids; Antigen-Antibody Reactions; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Oxygenases; Proline; Spectrophotometry | 1978 |
Characterization of the stabilizing effect of point mutations of pyruvate oxidase from Lactobacillus plantarum: protection of the native state by modulating coenzyme binding and subunit interaction.
Topics: Alanine; Amino Acid Sequence; Asparagine; Enzyme Stability; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Kinetics; Lactobacillus; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Proline; Protein Denaturation; Pyruvate Oxidase; Recombinant Proteins; Serine; Spectrophotometry, Ultraviolet; Thiamine Pyrophosphate; Urea; Valine | 1992 |
13C-NMR studies on the reaction intermediates of porcine kidney D-amino acid oxidase reconstituted with 13C-enriched flavin adenine dinucleotide.
Topics: Alanine; Animals; D-Amino-Acid Oxidase; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Kidney; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Proline; Spectrophotometry; Swine | 1987 |
Studies on the mechanism of action of D-amino acid oxidase. Evidence for removal of substrate -hydrogen as a proton.
Topics: Alanine; Chemical Phenomena; Chemistry; Chlorine; D-Amino-Acid Oxidase; Deuterium; Flavin-Adenine Dinucleotide; Hydrogen; Hydrogen-Ion Concentration; Keto Acids; Kinetics; Models, Chemical; Nitrogen; Oxygen; Phenylhydrazines; Proline; Protons; Pyruvates; Quaternary Ammonium Compounds; Serine; Spectrophotometry; Stereoisomerism; Thiosemicarbazones; Tritium; Ultraviolet Rays | 1971 |
On the structures of flavoprotein D-amino acid oxidase purple intermediates. A resonance Raman study.
Topics: Alanine; Animals; D-Amino-Acid Oxidase; Flavin-Adenine Dinucleotide; Flavoproteins; Kidney; Kinetics; Proline; Protein Binding; Protein Conformation; Spectrum Analysis, Raman; Swine | 1983 |
An amplified chemiluminescent assay for the detection of alkaline phosphatase.
Topics: Alkaline Phosphatase; D-Amino-Acid Oxidase; Enzyme Activation; Flavin-Adenine Dinucleotide; Horseradish Peroxidase; Hydrogen Peroxide; Kinetics; Luminescent Measurements; Luminol; Proline; Time Factors | 1995 |
The choice of reducing substrate is altered by replacement of an alanine by a proline in the FAD domain of a bispecific NAD(P)H-nitrate reductase from birch.
Topics: Alanine; Amino Acid Sequence; Binding Sites; Codon; Flavin-Adenine Dinucleotide; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NADP; Nitrate Reductase (NAD(P)H); Nitrate Reductases; Oxidation-Reduction; Proline; Recombinant Proteins; Sequence Homology, Amino Acid; Substrate Specificity; Trees | 1995 |
Conformational change and membrane association of the PutA protein are coincident with reduction of its FAD cofactor by proline.
Topics: Bacterial Proteins; Cell Membrane; Chymotrypsin; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Flavin-Adenine Dinucleotide; Membrane Proteins; Oxidation-Reduction; Proline; Protein Conformation | 1993 |
Cloning and functional expression of a mammalian gene for a peroxisomal sarcosine oxidase.
Topics: Amino Acid Sequence; Animals; Caenorhabditis elegans; Cell Line; Cloning, Molecular; DNA, Complementary; Flavin-Adenine Dinucleotide; Flavoproteins; Fluorescent Antibody Technique, Indirect; Humans; Kidney; Kinetics; Microbodies; Molecular Sequence Data; Oxidoreductases, N-Demethylating; Pipecolic Acids; Proline; Rabbits; Sarcosine; Sarcosine Oxidase; Sequence Alignment; Sequence Homology, Amino Acid; Subcellular Fractions | 1997 |
Regulation of gene expression by repressor localization: biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive.
Topics: Bacterial Proteins; Cell Membrane; DNA, Bacterial; Flavin-Adenine Dinucleotide; Gene Expression Regulation, Bacterial; Membrane Proteins; Mutation; Proline; Proline Oxidase; Protein Binding; Repressor Proteins; Salmonella typhimurium | 1997 |
Two-component flavin-dependent pyrrole-2-carboxylate monooxygenase from Rhodococcus sp.
Topics: Amino Acid Sequence; Cytochrome c Group; Electrophoresis, Polyacrylamide Gel; Flavin-Adenine Dinucleotide; Hydrogen Peroxide; Hydroxylation; Mixed Function Oxygenases; Molecular Sequence Data; NAD; Oxidation-Reduction; Oxidoreductases; Oxygen Consumption; Proline; Protein Conformation; Rhodococcus; Sequence Alignment; Sequence Analysis; Sequence Homology, Amino Acid | 1997 |
Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Flavin-Adenine Dinucleotide; Genetic Vectors; Glycine; Hydroxylation; Kinetics; Lysine; Mixed Function Oxygenases; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Proline; Sequence Homology, Amino Acid | 1999 |
Monomeric sarcosine oxidase: structure of a covalently flavinylated amine oxidizing enzyme.
Topics: Acetates; Allosteric Regulation; Amino Acid Sequence; Bacillus; Bacterial Proteins; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Models, Molecular; Molecular Sequence Data; Oxidoreductases, N-Demethylating; Proline; Protein Conformation; Recombinant Fusion Proteins; Sarcosine Oxidase; Sequence Alignment; Sequence Homology, Amino Acid | 1999 |
Regulation of flavin dehydrogenase compartmentalization: requirements for PutA-membrane association in Salmonella typhimurium.
Topics: Bacterial Proteins; Binding Sites; Electron Transport; Flavin-Adenine Dinucleotide; Liposomes; Membrane Lipids; Membrane Proteins; Oxidation-Reduction; Proline; Proline Oxidase; Quinones; Salmonella typhimurium | 1999 |
Effects of proline analog binding on the spectroscopic and redox properties of PutA.
Topics: Bacterial Proteins; Binding Sites; Escherichia coli; Escherichia coli Proteins; Flavin-Adenine Dinucleotide; Kinetics; Membrane Proteins; Oxidation-Reduction; Potentiometry; Proline; Spectrophotometry | 2002 |
Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman spectroscopy.
Topics: Acyl Coenzyme A; Acyl-CoA Dehydrogenase; Animals; Binding Sites; Catalysis; Flavin-Adenine Dinucleotide; Glutamic Acid; Glutamine; Hydrogen Bonding; Kinetics; Mutagenesis, Site-Directed; Potentiometry; Proline; Protons; Recombinant Proteins; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Swine | 2003 |
The structure of the S127P mutant of cytochrome b5 reductase that causes methemoglobinemia shows the AMP moiety of the flavin occupying the substrate binding site.
Topics: Adenosine Monophosphate; Amino Acid Substitution; Animals; Binding Sites; Crystallography, X-Ray; Cytochrome-B(5) Reductase; Flavin-Adenine Dinucleotide; Humans; Kinetics; Methemoglobinemia; Mutagenesis, Site-Directed; NAD; Proline; Protein Conformation; Rats; Recombinant Proteins; Serine; Spectrophotometry, Ultraviolet; Substrate Specificity | 2003 |
Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors.
Topics: Bacterial Proteins; Binding, Competitive; Cloning, Molecular; Crystallography, X-Ray; Enzyme Inhibitors; Enzyme Stability; Escherichia coli Proteins; Flavin-Adenine Dinucleotide; Furans; Humans; Leucine; Macromolecular Substances; Membrane Proteins; Methylenetetrahydrofolate Reductase (NADPH2); Models, Molecular; Mutagenesis, Site-Directed; Peptide Fragments; Proline; Proline Oxidase; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary | 2004 |
Regulation of PutA-membrane associations by flavin adenine dinucleotide reduction.
Topics: Bacterial Proteins; DNA-Binding Proteins; Escherichia coli Proteins; Flavin-Adenine Dinucleotide; Intracellular Fluid; Ligands; Lipid Bilayers; Membrane Proteins; Oxidation-Reduction; Proline; Proline Oxidase; Protein Binding; Static Electricity; Substrate Specificity | 2004 |
Effect of osmolytes on the interaction of flavin adenine dinucleotide with muscle glycogen phosphorylase b.
Topics: Animals; Betaine; Flavin-Adenine Dinucleotide; Glycogen Phosphorylase, Muscle Form; Methylamines; Osmolar Concentration; Phosphorylase b; Proline; Protein Binding; Rabbits | 2005 |
Functional consequences of PRODH missense mutations.
Topics: Alleles; Amino Acid Sequence; Catalytic Domain; Cloning, Molecular; Flavin-Adenine Dinucleotide; Humans; In Vitro Techniques; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation, Missense; Phenotype; Proline; Proline Oxidase; Recombinant Proteins; Schizophrenia; Sequence Homology, Amino Acid | 2005 |
Cytochrome b5 reductase: role of the si-face residues, proline 92 and tyrosine 93, in structure and catalysis.
Topics: Amino Acid Motifs; Amino Acid Substitution; Animals; Catalysis; Circular Dichroism; Cytochrome-B(5) Reductase; Enzyme Activation; Flavin-Adenine Dinucleotide; Flavins; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Mutagenesis, Site-Directed; Oxidation-Reduction; Potentiometry; Proline; Rats; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Thermodynamics; Tyrosine | 2005 |
Characterization of a bifunctional PutA homologue from Bradyrhizobium japonicum and identification of an active site residue that modulates proline reduction of the flavin adenine dinucleotide cofactor.
Topics: Alanine; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Bradyrhizobium; Cell Membrane; Flavin-Adenine Dinucleotide; Kinetics; Ligands; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Phospholipids; Proline; Proline Oxidase; Sequence Alignment; Titrimetry | 2005 |
Structure and kinetics of monofunctional proline dehydrogenase from Thermus thermophilus.
Topics: Catalysis; Crystallization; Crystallography, X-Ray; Flavin-Adenine Dinucleotide; Kinetics; Models, Chemical; Models, Molecular; Proline; Proline Oxidase; Protein Structure, Tertiary; Reactive Oxygen Species; Thermus thermophilus | 2007 |
Mechanistic aspects and redox properties of hyperthermophilic L-proline dehydrogenase from Pyrococcus furiosus related to dimethylglycine dehydrogenase/oxidase.
Topics: Amino Acid Sequence; Binding Sites; Dimethylglycine Dehydrogenase; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Pipecolic Acids; Proline; Proline Oxidase; Protein Subunits; Pyrococcus furiosus; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Temperature | 2007 |
The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution.
Topics: Amino Acid Sequence; Aspergillus niger; Binding Sites; Biocatalysis; Catalytic Domain; Directed Molecular Evolution; Flavin-Adenine Dinucleotide; Humans; Hydrophobic and Hydrophilic Interactions; Isomerism; Molecular Sequence Data; Monoamine Oxidase; Mutant Proteins; Mutation; Oxidation-Reduction; Proline; Protein Structure, Secondary; Sequence Alignment; Static Electricity; Substrate Specificity | 2008 |
Characterization of a novel dye-linked L-proline dehydrogenase from an aerobic hyperthermophilic archaeon, Pyrobaculum calidifontis.
Topics: Amino Acid Sequence; Chromatography; Cloning, Molecular; Coenzymes; Enzyme Stability; Escherichia coli; Flavin-Adenine Dinucleotide; Hot Temperature; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Molecular Weight; Proline; Proline Oxidase; Protein Multimerization; Pyrobaculum; Sequence Alignment | 2011 |
Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein.
Topics: 1-Pyrroline-5-Carboxylate Dehydrogenase; Anaerobiosis; Bacterial Proteins; Bradyrhizobium; Catalysis; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Flavin-Adenine Dinucleotide; Glutamic Acid; Homeostasis; Isomerism; Kinetics; Membrane Proteins; Oxidation-Reduction; Proline; Proline Oxidase; Protein Multimerization; Protein Structure, Tertiary | 2012 |
Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi.
Topics: Amino Acid Sequence; Animals; Down-Regulation; Electron Transport; Flavin-Adenine Dinucleotide; Intracellular Space; Life Cycle Stages; Molecular Sequence Data; Oxidative Stress; Proline; Proline Oxidase; Protein Transport; Trypanosoma cruzi | 2013 |
Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria.
Topics: Biocatalysis; Catalytic Domain; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Flavoproteins; Furans; Humans; Hydroxyproline; Hyperoxaluria, Primary; Ligands; Models, Molecular; Mutant Proteins; Peptide Fragments; Proline; Proline Oxidase; Protein Conformation; Recombinant Proteins; Substrate Specificity; Terminology as Topic; Ubiquinone | 2015 |
Computational insights on the hydride and proton transfer mechanisms of L-proline dehydrogenase.
Topics: Flavin-Adenine Dinucleotide; Kinetics; Oxidation-Reduction; Oxidoreductases; Proline; Proline Oxidase; Protons | 2023 |