Page last updated: 2024-09-03

methyl phenylglycine and aminopenicillanic acid

methyl phenylglycine has been researched along with aminopenicillanic acid in 3 studies

Compound Research Comparison

Studies
(methyl phenylglycine)
Trials
(methyl phenylglycine)
Recent Studies (post-2010)
(methyl phenylglycine)
Studies
(aminopenicillanic acid)
Trials
(aminopenicillanic acid)
Recent Studies (post-2010) (aminopenicillanic acid)
2608208038

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's3 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Svedas, VK; Youshko, MI1
Alonso, J; Fernández-Lafuente, R; Fernández-Lorente, G; García-López, JL; Guisan, JM; Hernández-Jústiz, O; Mateo, C; Moreno, MA; Terreni, M1
Gabor, EM; Janssen, DB1

Other Studies

3 other study(ies) available for methyl phenylglycine and aminopenicillanic acid

ArticleYear
Kinetics of ampicillin synthesis catalyzed by penicillin acylase from E. coli in homogeneous and heterogeneous systems. Quantitative characterization of nucleophile reactivity and mathematical modeling of the process.
    Biochemistry. Biokhimiia, 2000, Volume: 65, Issue:12

    Topics: Ampicillin; Escherichia coli; Glycine; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Models, Theoretical; Penicillanic Acid; Penicillin Amidase; Temperature

2000
Biotransformations catalyzed by multimeric enzymes: stabilization of tetrameric ampicillin acylase permits the optimization of ampicillin synthesis under dissociation conditions.
    Biomacromolecules, 2001,Spring, Volume: 2, Issue:1

    Topics: Acetobacter; Ampicillin; Bioreactors; Catalysis; Enzyme Stability; Enzymes, Immobilized; Escherichia coli; Glycine; Hydrogen-Ion Concentration; Kinetics; Methanol; Molecular Structure; Penicillanic Acid; Penicillin Amidase; Phosphates; Protein Structure, Quaternary; Temperature

2001
Increasing the synthetic performance of penicillin acylase PAS2 by structure-inspired semi-random mutagenesis.
    Protein engineering, design & selection : PEDS, 2004, Volume: 17, Issue:7

    Topics: beta-Lactams; Catalysis; Chromatography, High Pressure Liquid; Dose-Response Relationship, Drug; Escherichia coli; Genetic Techniques; Glycine; Hydrolysis; Kinetics; Models, Chemical; Mutagenesis; Mutation; Penicillanic Acid; Penicillin Amidase; Plasmids; Protein Conformation; Protein Engineering; Time Factors

2004