Compounds > proline

proline and flavin mononucleotide

proline has been researched along with flavin mononucleotide in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19902 (40.00)18.7374
1990's2 (40.00)18.2507
2000's1 (20.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Cecchini, G; Kearney, EB; Lipsick, J; Perl, M; Singer, TP1
Miura, R; Miyake, Y1
Bisch, D; Blanche, F; Debussche, L; Faucher, D; Ratet, N; Thibaut, D1
Curley, GP; Knauf, MA; Löhr, F; Mayhew, SG; Müller, F; O'Farrell, P; Rüterjans, H1
Aufhammer, SW; Ermler, U; Hagemeier, CH; Shima, S; Thauer, RK; Warkentin, E1

Other Studies

5 other study(ies) available for proline and flavin mononucleotide

ArticleYear
Transport and binding of riboflavin by Bacillus subtilis.
    The Journal of biological chemistry, 1979, Aug-10, Volume: 254, Issue:15

    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.
    Journal of biochemistry, 1987, Volume: 102, Issue:6

    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.
    Journal of bacteriology, 1995, Volume: 177, Issue:18

    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.
    European journal of biochemistry, 1993, Apr-01, Volume: 213, Issue:1

    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.
    Protein science : a publication of the Protein Society, 2005, Volume: 14, Issue:7

    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