proline has been researched along with flavin mononucleotide in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (40.00) | 18.7374 |
1990's | 2 (40.00) | 18.2507 |
2000's | 1 (20.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Cecchini, G; Kearney, EB; Lipsick, J; Perl, M; Singer, TP | 1 |
Miura, R; Miyake, Y | 1 |
Bisch, D; Blanche, F; Debussche, L; Faucher, D; Ratet, N; Thibaut, D | 1 |
Curley, GP; Knauf, MA; Löhr, F; Mayhew, SG; Müller, F; O'Farrell, P; Rüterjans, H | 1 |
Aufhammer, SW; Ermler, U; Hagemeier, CH; Shima, S; Thauer, RK; Warkentin, E | 1 |
5 other study(ies) available for proline and flavin mononucleotide
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 |
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 |
Purification of the two-enzyme system catalyzing the oxidation of the D-proline residue of pristinamycin IIB during the last step of pristinamycin IIA biosynthesis.
Topics: Amino Acid Sequence; Flavin Mononucleotide; FMN Reductase; Mixed Function Oxygenases; Models, Chemical; Molecular Sequence Data; Molecular Weight; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxidoreductases; Oxygen Consumption; Oxygenases; Proline; Streptomyces; Substrate Specificity; Virginiamycin | 1995 |
Homonuclear and heteronuclear NMR studies of oxidized Desulfovibrio vulgaris flavodoxin. Sequential assignments and identification of secondary structure elements.
Topics: Amino Acid Sequence; Binding Sites; Desulfovibrio vulgaris; Flavin Mononucleotide; Flavins; Flavodoxin; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Nitrogen Isotopes; Oxidation-Reduction; Proline; Protein Structure, Secondary; Recombinant Proteins; Solutions | 1993 |
Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420: Architecture of the F420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalysis; Crystallography, X-Ray; Flavin Mononucleotide; Flavins; Luciferases; Methanobacterium; Models, Molecular; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Peptides; Proline; Protein Binding; Protein Conformation; Riboflavin; Sequence Homology, Amino Acid | 2005 |