selenocysteine and pyridoxal phosphate

selenocysteine has been researched along with pyridoxal phosphate in 12 studies

Research

Studies (12)

TimeframeStudies, this research(%)All Research%
pre-19903 (25.00)18.7374
1990's3 (25.00)18.2507
2000's3 (25.00)29.6817
2010's2 (16.67)24.3611
2020's1 (8.33)2.80

Authors

AuthorsStudies
Beilstein, MA; Whanger, PD1
Böck, A; Boesmiller, K; Forchhammer, K1
Chocat, P; Esaki, N; Nakamura, T; Soda, K; Tanaka, H1
Chocat, P; Esaki, N; Karai, N; Nakamura, T; Soda, K; Tanaka, H1
Esaki, N; Karai, N; Soda, K; Tanaka, H1
Lacourciere, GM; Stadtman, TC1
Esaki, N; Kurihara, T; Mihara, H; Yoshimura, T1
Esaki, N; Fujii, T; Hata, Y; Kato, S; Kurihara, T; Mihara, H1
Bittner, F; Heidenreich, T; Mendel, RR; Wollers, S1
Cassago, A; da Silva, MT; Manzine, LR; Thiemann, OH1
Bröcker, MJ; Hammond, G; Itoh, Y; Sekine, S; Söll, D; Suetsugu, S; Yokoyama, S1
Makarova, NE; Manta, B; Mariotti, M1

Reviews

1 review(s) available for selenocysteine and pyridoxal phosphate

ArticleYear
The selenophosphate synthetase family: A review.
    Free radical biology & medicine, 2022, 11-01, Volume: 192

    Topics: Adenosine Triphosphate; Cysteine; Hormones; Ligases; Phosphates; Phosphotransferases; Pyridoxal Phosphate; Selenium; Selenium Compounds; Selenocysteine; Selenoproteins

2022

Other Studies

11 other study(ies) available for selenocysteine and pyridoxal phosphate

ArticleYear
Selenium metabolism and glutathione peroxidase activity in cultured human lymphoblasts. Effects of transsulfuration defects and pyridoxal phosphate.
    Biological trace element research, 1992, Volume: 35, Issue:2

    Topics: Cell Division; Cell Line; Enzyme Induction; Glutathione Peroxidase; Humans; Lymphocytes; Mutation; Pyridoxal Phosphate; Selenium; Selenocysteine; Selenomethionine

1992
The function of selenocysteine synthase and SELB in the synthesis and incorporation of selenocysteine.
    Biochimie, 1991, Volume: 73, Issue:12

    Topics: Bacterial Proteins; Binding Sites; Chromatography, Thin Layer; Cysteine; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Organoselenium Compounds; Oxidation-Reduction; Protein Biosynthesis; Pyridoxal Phosphate; RNA, Transfer, Amino Acid-Specific; RNA, Transfer, Amino Acyl; Selenocysteine; Transferases

1991
Microbial distribution of selenocysteine lyase.
    Journal of bacteriology, 1983, Volume: 156, Issue:1

    Topics: Alcaligenes; Bacteria; Cysteine; Cytoplasm; Fungi; Kinetics; Lyases; Pseudomonas; Pyridoxal Phosphate; Selenium; Selenocysteine; Yeasts

1983
Selenocysteine beta-lyase: a novel pyridoxal enzyme.
    Progress in clinical and biological research, 1984, Volume: 144A

    Topics: Animals; Bacteria; Cysteine; Hydrogen-Ion Concentration; Liver; Lyases; Pyridoxal Phosphate; Selenium; Selenocysteine; Substrate Specificity; Swine; Tissue Distribution

1984
Reaction and regulation mechanisms of selenocysteine beta-lyase.
    Progress in clinical and biological research, 1984, Volume: 144A

    Topics: Aluminum; Animals; Cysteine; Dithiothreitol; Keto Acids; Liver; Lyases; Magnetic Resonance Spectroscopy; Pyridoxal Phosphate; Pyridoxamine; Selenium; Selenocysteine; Swine

1984
The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate.
    The Journal of biological chemistry, 1998, Nov-20, Volume: 273, Issue:47

    Topics: Azotobacter vinelandii; Bacterial Proteins; Carbon-Sulfur Lyases; Drosophila Proteins; Lyases; Models, Chemical; Nuclear Magnetic Resonance, Biomolecular; Phosphates; Phosphorus Isotopes; Phosphotransferases; Pyridoxal Phosphate; Selenium Compounds; Selenocysteine; Substrate Specificity

1998
Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions.
    Journal of biochemistry, 2000, Volume: 127, Issue:4

    Topics: Bacterial Proteins; Carbon-Sulfur Lyases; Escherichia coli; Kinetics; Lyases; Mutation; Pyridoxal Phosphate; Pyruvic Acid; Selenocysteine; Spectrophotometry; Substrate Specificity

2000
Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine.
    Journal of biochemistry, 2002, Volume: 131, Issue:5

    Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Binding Sites; Carbon-Sulfur Lyases; Crystallography, X-Ray; Cysteine; Escherichia coli; Lyases; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Pyridoxal Phosphate; Selenocysteine; Sequence Homology, Amino Acid; Substrate Specificity

2002
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration.
    The Journal of biological chemistry, 2005, Feb-11, Volume: 280, Issue:6

    Topics: Aldehyde Oxidase; Arabidopsis; Arabidopsis Proteins; Bacterial Proteins; Binding Sites; Catalysis; Coenzymes; Cysteine; Cytosol; Fluorescent Dyes; Genetic Vectors; Iron-Sulfur Proteins; Kinetics; Lyases; Lysine; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Naphthalenesulfonates; Pichia; Plant Proteins; Protein Binding; Protein Structure, Tertiary; Pteridines; Pyridoxal Phosphate; Selenocysteine; Spectrophotometry; Substrate Specificity; Sulfides; Sulfurtransferases; Xanthine Dehydrogenase

2005
An efficient protocol for the production of tRNA-free recombinant Selenocysteine Synthase (SELA) from Escherichia coli and its biophysical characterization.
    Protein expression and purification, 2013, Volume: 88, Issue:1

    Topics: Biophysics; Escherichia coli; Molecular Weight; Protein Structure, Secondary; Pyridoxal Phosphate; Recombinant Proteins; RNA, Transfer, Amino Acid-Specific; Selenocysteine; Transferases

2013
Decameric SelA•tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation.
    Science (New York, N.Y.), 2013, Apr-05, Volume: 340, Issue:6128

    Topics: Arginine; Bacteria; Bacterial Proteins; Catalysis; Catalytic Domain; Crystallography, X-Ray; Protein Multimerization; Protein Structure, Secondary; Protein Structure, Tertiary; Pyridoxal Phosphate; RNA, Transfer, Amino Acyl; Selenocysteine; Transferases

2013