3-phenylpropionic acid and maleic acid

3-phenylpropionic acid has been researched along with maleic acid in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (75.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Jansonius, JN; Kirsch, JF; Malashkevich, VN; Onuffer, JJ1
Berger, JM; Chow, MA; Corbett, KD; Kirsch, JF; McElroy, KE1
Kirsch, JF; Onuffer, JJ1
Hayashi, H; Hirotsu, K; Kagamiyama, H; Nakai, Y; Okamoto, A1

Other Studies

4 other study(ies) available for 3-phenylpropionic acid and maleic acid

ArticleYear
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
    Nature structural biology, 1995, Volume: 2, Issue:7

    Topics: Arginine; Aspartate Aminotransferases; Binding Sites; Crystallography, X-Ray; Escherichia coli; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Structure-Activity Relationship; Substrate Specificity; Tyrosine Transaminase

1995
Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase.
    Biochemistry, 2004, Oct-12, Volume: 43, Issue:40

    Topics: Alanine; Aspartate Aminotransferases; Crystallography, X-Ray; Directed Molecular Evolution; Escherichia coli; Kinetics; Models, Molecular; Mutation; Protein Structure, Tertiary; Substrate Specificity; Tyrosine Transaminase

2004
Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.
    Protein science : a publication of the Protein Society, 1995, Volume: 4, Issue:9

    Topics: Aspartate Aminotransferases; Binding Sites; Drug Design; Enzyme Inhibitors; Escherichia coli; Kinetics; Maleates; Molecular Structure; Mutagenesis, Site-Directed; Phenylalanine; Phenylpropionates; Protein Conformation; Sequence Homology; Substrate Specificity; Tyrosine Transaminase

1995
Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network.
    Journal of molecular biology, 1998, Jul-17, Volume: 280, Issue:3

    Topics: Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Enzyme Inhibitors; Hydrogen Bonding; Maleates; Models, Molecular; Paracoccus denitrificans; Phenylpropionates; Protein Conformation; Substrate Specificity; Transaminases

1998