Compounds > alanine

alanine and 4-nitrophenylphosphate

alanine has been researched along with 4-nitrophenylphosphate in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19901 (20.00)18.7374
1990's1 (20.00)18.2507
2000's3 (60.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Choy, PC; Hatch, GM1
Kantrowitz, ER; Xu, X1
Catrina, IE; Hengge, AC; Holtz, KM; Kantrowitz, ER1
Crisma, M; Felluga, F; Formaggio, F; Rossi, P; Scrimin, P; Tecilla, P; Toniolo, C1
Hausmann, S; Shuman, S1

Other Studies

5 other study(ies) available for alanine and 4-nitrophenylphosphate

ArticleYear
Phosphocholine phosphatase and alkaline phosphatase are different enzymes in hamster heart.
    Lipids, 1987, Volume: 22, Issue:9

    Topics: Alanine; Alkaline Phosphatase; Animals; Cricetinae; Hydrogen-Ion Concentration; Kinetics; Male; Mesocricetus; Myocardium; Nitrophenols; Organophosphorus Compounds; Phenylalanine; Phosphoric Monoester Hydrolases

1987
Binding of magnesium in a mutant Escherichia coli alkaline phosphatase changes the rate-determining step in the reaction mechanism.
    Biochemistry, 1993, Oct-12, Volume: 32, Issue:40

    Topics: Alanine; Alkaline Phosphatase; Amino Acid Sequence; Aspartic Acid; Binding Sites; Escherichia coli; Glutamates; Glutamic Acid; Kinetics; Magnesium; Mutagenesis, Site-Directed; Nitrophenols; Organophosphorus Compounds; Protein Conformation; Recombinant Proteins; Zinc

1993
Mutation of Arg-166 of alkaline phosphatase alters the thio effect but not the transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatases.
    Biochemistry, 2000, Aug-08, Volume: 39, Issue:31

    Topics: Alanine; Alkaline Phosphatase; Arginine; Enzyme Inhibitors; Escherichia coli; Hydrolysis; Kinetics; Linear Energy Transfer; Mutagenesis, Site-Directed; Nitrophenols; Organophosphorus Compounds; Organothiophosphorus Compounds; Phosphates; Substrate Specificity; Thionucleotides

2000
An azacrown-functionalized peptide as a metal ion based catalyst for the cleavage of a RNA-model substrate.
    Biopolymers, 2000, Volume: 55, Issue:6

    Topics: Alanine; Catalysis; Heterocyclic Compounds, 1-Ring; Kinetics; Metals; Models, Molecular; Molecular Structure; Nitrophenols; Organophosphates; Organophosphorus Compounds; Peptides; Protein Binding; Protein Structure, Secondary; RNA; Spectroscopy, Fourier Transform Infrared; Temperature; Zinc

2000
Defining the active site of Schizosaccharomyces pombe C-terminal domain phosphatase Fcp1.
    The Journal of biological chemistry, 2003, Apr-18, Volume: 278, Issue:16

    Topics: Alanine; Amino Acid Sequence; Amino Acids; Arginine; Aspartic Acid; Binding Sites; Catalytic Domain; DNA Mutational Analysis; Dose-Response Relationship, Drug; Gene Deletion; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nitrophenols; Organophosphorus Compounds; Phosphoprotein Phosphatases; Protein Structure, Tertiary; Schizosaccharomyces; Sequence Homology, Amino Acid

2003