Compounds > arginine

arginine and adenylosuccinate

arginine has been researched along with adenylosuccinate in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's4 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Brosius, JL; Colman, RF1
Colman, RF; Palenchar, JB1
Colman, RF; Segall, ML1
Colman, RF; Cowley, D; McGown, I; Patterson, D; Sivendran, S; Spiegel, E1

Other Studies

4 other study(ies) available for arginine and adenylosuccinate

ArticleYear
Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required.
    Biochemistry, 2002, Feb-19, Volume: 41, Issue:7

    Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Alanine; Amino Acid Substitution; Arginine; Bacillus subtilis; Binding Sites; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Genetic Complementation Test; Glutamic Acid; Kinetics; Light; Lysine; Molecular Weight; Mutagenesis, Site-Directed; Peptide Fragments; Protein Structure, Secondary; Scattering, Radiation; Tritium

2002
Characterization of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase deficiency: asparagine 276 plays an important structural role.
    Biochemistry, 2003, Feb-25, Volume: 42, Issue:7

    Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Aminoimidazole Carboxamide; Arginine; Asparagine; Bacillus subtilis; Bacterial Proteins; Circular Dichroism; Enzyme Activation; Humans; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Ribonucleotides; Substrate Specificity; Threonine

2003
Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis.
    Biochemistry, 2004, Jun-15, Volume: 43, Issue:23

    Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Animals; Arginine; Asparagine; Bacillus subtilis; Binding Sites; Catalysis; Circular Dichroism; Glutamine; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Sequence Alignment; Thermodynamics

2004
Two novel mutant human adenylosuccinate lyases (ASLs) associated with autism and characterization of the equivalent mutant Bacillus subtilis ASL.
    The Journal of biological chemistry, 2004, Dec-17, Volume: 279, Issue:51

    Topics: Adenosine Monophosphate; Adenylosuccinate Lyase; Amino Acid Sequence; Arginine; Aspartic Acid; Autistic Disorder; Bacillus subtilis; Circular Dichroism; DNA; Electrophoresis, Polyacrylamide Gel; Family Health; Female; Glutamic Acid; Heterozygote; Hot Temperature; Humans; Hydrogen-Ion Concentration; Kinetics; Male; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mothers; Mutagenesis, Site-Directed; Mutation; Polymerase Chain Reaction; Protein Binding; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Spectrophotometry; Temperature; Thermotoga maritima; Time Factors; Ultraviolet Rays

2004