Compounds > glutamine

glutamine and adenylyl imidodiphosphate

glutamine has been researched along with adenylyl imidodiphosphate in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (60.00)18.2507
2000's1 (20.00)29.6817
2010's1 (20.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Eisenberg, D; Liaw, SH1
Chang, S; Hsieh, T; Hu, T1
Maxwell, A; Smith, CV1
Abramczyk, BA; Gursky, SK; Postel, EH; Xu, Y1
Brunzelle, JS; Grum-Tokars, V; McNamara, LK; Schavocky, JP; Watterson, DM1

Other Studies

5 other study(ies) available for glutamine and adenylyl imidodiphosphate

ArticleYear
Structural model for the reaction mechanism of glutamine synthetase, based on five crystal structures of enzyme-substrate complexes.
    Biochemistry, 1994, Jan-25, Volume: 33, Issue:3

    Topics: Adenylyl Imidodiphosphate; Crystallography, X-Ray; Glutamate-Ammonia Ligase; Glutamates; Glutamic Acid; Glutamine; Methionine Sulfoximine; Models, Chemical; Models, Molecular; Protein Conformation; Quaternary Ammonium Compounds; Salmonella typhimurium

1994
Identifying Lys359 as a critical residue for the ATP-dependent reactions of Drosophila DNA topoisomerase II.
    The Journal of biological chemistry, 1998, Apr-17, Volume: 273, Issue:16

    Topics: Adenosine Triphosphate; Adenylyl Imidodiphosphate; Amino Acid Sequence; Amino Acid Substitution; Animals; Base Sequence; Binding Sites; DNA; DNA Topoisomerases, Type II; DNA, Circular; Drosophila; Glutamic Acid; Glutamine; Kinetics; Lysine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity

1998
Identification of a residue involved in transition-state stabilization in the ATPase reaction of DNA gyrase.
    Biochemistry, 1998, Jul-07, Volume: 37, Issue:27

    Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Circular Dichroism; Coumarins; Cross-Linking Reagents; Crystallography, X-Ray; Dimethyl Suberimidate; DNA Gyrase; DNA Topoisomerases, Type II; Enzyme Stability; Glutamine; Hydrolysis; Lysine; Models, Molecular; Molecular Weight; Mutagenesis, Site-Directed; Protein Binding

1998
Structure-based mutational and functional analysis identify human NM23-H2 as a multifunctional enzyme.
    Biochemistry, 2002, May-21, Volume: 41, Issue:20

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Binding Sites; Catalysis; DNA; DNA-Binding Proteins; Glutamine; Histidine; Humans; Hydrolysis; Monomeric GTP-Binding Proteins; Multienzyme Complexes; Mutagenesis, Site-Directed; NM23 Nucleoside Diphosphate Kinases; Nucleoside-Diphosphate Kinase; Structure-Activity Relationship; Transcription Factors

2002
Site-directed mutagenesis of the glycine-rich loop of death associated protein kinase (DAPK) identifies it as a key structure for catalytic activity.
    Biochimica et biophysica acta, 2011, Volume: 1813, Issue:5

    Topics: Adenosine Diphosphate; Adenylyl Imidodiphosphate; Amino Acid Sequence; Apoptosis Regulatory Proteins; Binding Sites; Biocatalysis; Calcium-Calmodulin-Dependent Protein Kinases; Crystallography, X-Ray; Death-Associated Protein Kinases; Enzyme Assays; Glutamine; Kinetics; Ligands; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutant Proteins; Mutation; Protein Structure, Secondary; Sequence Alignment; Structure-Activity Relationship; Valine

2011