Compounds > carbamyl phosphate

carbamyl phosphate and succinic acid

carbamyl phosphate has been researched along with succinic acid in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19902 (25.00)18.7374
1990's6 (75.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Cunin, R; Hervé, G; Ladjimi, MM; Van Vliet, F; Xi, XG1
Kleanthous, C; Schachman, HK; Wemmer, DE1
Gouaux, JE; Lipscomb, WN1
Baker, DP; Fetler, L; Kantrowitz, ER; Keiser, RT; Vachette, P1
England, P; Hervé, G; Leconte, C; Tauc, P1
Amemiya, Y; Kihara, H; Moody, MF; Sano, T; Tsuruta, H; Vachette, P; Wakabayashi, K1
Lum, L; Schachman, HK; Waldrop, GL; Zhou, BB1
Burns, BP; Hazell, SL; Mendz, GL1

Other Studies

8 other study(ies) available for carbamyl phosphate and succinic acid

ArticleYear
The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate.
    Biochemistry, 1990, Sep-11, Volume: 29, Issue:36

    Topics: Amino Acid Sequence; Aspartate Carbamoyltransferase; Aspartic Acid; Bacterial Proteins; Binding Sites; Carbamyl Phosphate; Catalysis; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Protein Binding; Substrate Specificity; Succinates; Succinic Acid

1990
The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase.
    The Journal of biological chemistry, 1988, Sep-15, Volume: 263, Issue:26

    Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Phosphonoacetic Acid; Succinates; Succinic Acid

1988
Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase.
    Proceedings of the National Academy of Sciences of the United States of America, 1988, Volume: 85, Issue:12

    Topics: Aspartate Carbamoyltransferase; Binding Sites; Carbamates; Carbamyl Phosphate; Models, Molecular; Protein Binding; Protein Conformation; Succinates; Succinic Acid; X-Ray Diffraction

1988
Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase.
    Protein science : a publication of the Protein Society, 1995, Volume: 4, Issue:2

    Topics: Adenosine Triphosphate; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Kinetics; Mutagenesis; Point Mutation; Protein Conformation; Scattering, Radiation; Structure-Activity Relationship; Substrate Specificity; Succinates; Succinic Acid; Uridine Triphosphate; X-Rays

1995
Apparent cooperativity for carbamoylphosphate in Escherichia coli aspartate transcarbamoylase only reflects cooperativity for aspartate.
    European journal of biochemistry, 1994, Jun-15, Volume: 222, Issue:3

    Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Dialysis; Escherichia coli; Substrate Specificity; Succinates; Succinic Acid

1994
Kinetics of the quaternary structure change of aspartate transcarbamylase triggered by succinate, a competitive inhibitor.
    Biochemistry, 1994, Aug-23, Volume: 33, Issue:33

    Topics: Aspartate Carbamoyltransferase; Binding, Competitive; Carbamyl Phosphate; Escherichia coli; Kinetics; Protein Conformation; Scattering, Radiation; Succinates; Succinic Acid; X-Rays

1994
A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.
    Protein science : a publication of the Protein Society, 1994, Volume: 3, Issue:6

    Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Carbon Isotopes; Catalysis; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Peptide Fragments; Phosphonoacetic Acid; Structure-Activity Relationship; Succinates; Succinic Acid; Zinc

1994
In situ properties of Helicobacter pylori aspartate carbamoyltransferase.
    Archives of biochemistry and biophysics, 1997, Nov-01, Volume: 347, Issue:1

    Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cytidine Triphosphate; Enzyme Inhibitors; Helicobacter pylori; Humans; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Maleates; Organophosphates; Phosphonoacetic Acid; Ribose; Stereoisomerism; Substrate Specificity; Succinic Acid; Temperature

1997