Page last updated: 2024-08-17

aspartic acid and phosphinothricin

aspartic acid has been researched along with phosphinothricin in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Crespo, JL; Florencio, FJ; Guerrero, MG	1
Eisenberg, D; Gill, HS	1

Other Studies

2 other study(ies) available for aspartic acid and phosphinothricin

Article	Year
Mutational analysis of Asp51 of Anabaena azollae glutamine synthetase. D51E mutation confers resistance to the active site inhibitors L-methionine-DL-sulfoximine and phosphinothricin. European journal of biochemistry, 1999, Volume: 266, Issue:3 Topics: Amino Acid Sequence; Aminobutyrates; Anabaena; Aspartic Acid; Base Sequence; Catalytic Domain; Cloning, Molecular; DNA Primers; Enzyme Inhibitors; Escherichia coli; Genes, Bacterial; Genetic Complementation Test; Glutamate-Ammonia Ligase; Herbicides; Kinetics; Methionine Sulfoximine; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Sequence Homology, Amino Acid	1999
The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition. Biochemistry, 2001, Feb-20, Volume: 40, Issue:7 Topics: Aminobutyrates; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Computer Simulation; Crystallography, X-Ray; Electrons; Enzyme Inhibitors; Glutamate-Ammonia Ligase; Glutamic Acid; Models, Molecular; Salmonella typhimurium; Spectroscopy, Fourier Transform Infrared; Static Electricity; Substrate Specificity; Thallium; Tyrosine	2001

Article

Year

Mutational analysis of Asp51 of Anabaena azollae glutamine synthetase. D51E mutation confers resistance to the active site inhibitors L-methionine-DL-sulfoximine and phosphinothricin.

European journal of biochemistry, 1999, Volume: 266, Issue:3

Topics: Amino Acid Sequence; Aminobutyrates; Anabaena; Aspartic Acid; Base Sequence; Catalytic Domain; Cloning, Molecular; DNA Primers; Enzyme Inhibitors; Escherichia coli; Genes, Bacterial; Genetic Complementation Test; Glutamate-Ammonia Ligase; Herbicides; Kinetics; Methionine Sulfoximine; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Sequence Homology, Amino Acid

1999

The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition.

Biochemistry, 2001, Feb-20, Volume: 40, Issue:7

Topics: Aminobutyrates; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Computer Simulation; Crystallography, X-Ray; Electrons; Enzyme Inhibitors; Glutamate-Ammonia Ligase; Glutamic Acid; Models, Molecular; Salmonella typhimurium; Spectroscopy, Fourier Transform Infrared; Static Electricity; Substrate Specificity; Thallium; Tyrosine

2001