carbamyl phosphate has been researched along with aspartic acid in 56 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 27 (48.21) | 18.7374 |
1990's | 24 (42.86) | 18.2507 |
2000's | 4 (7.14) | 29.6817 |
2010's | 1 (1.79) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Opella, SJ; Phillips, HM; Roberts, MF; Schaffer, MH; Stark, GR | 1 |
Allwell, NM; Hofmann, GE; Lennick, M; Zaug, A | 1 |
Dembo, M; Rubinow, SI | 1 |
Howlett, GJ; Schachman, HK | 1 |
Allewell, NM; Knier, BL | 1 |
Chan, WW; Enns, CA | 1 |
Christopherson, RI; Finch, LR | 1 |
Butterworth, PJ; Grayson, JE; Yon, RJ | 1 |
Goldin, A; Inouye, T; Johnson, RK; Stark, GR | 1 |
Kidder, GW; Nolan, LL | 1 |
Krebs, HA | 1 |
Jyssum, S | 1 |
Kantrowitz, ER; Newton, CJ; Stevens, RC | 1 |
Schachman, HK; Turnbull, JL; Waldrop, GL | 1 |
Cleland, WW; O'Leary, MH; Parmentier, LE; Schachman, HK | 1 |
Cleland, WW; Lee, S; O'Leary, MH; Parmentier, LE; Schachman, HK; Turnbull, JL; Waldrop, GL | 1 |
Schachman, HK; Wente, SR | 1 |
Kantrowitz, ER; Middleton, SA; Tauc, P; Vachette, P | 1 |
Eisenstein, E; Markby, DW; Schachman, HK | 1 |
Cunin, R; Hervé, G; Ladjimi, MM; Van Vliet, F; Xi, XG | 1 |
Kantrowitz, ER; Xu, W | 1 |
Hsuanyu, Y; Kantrowitz, ER; Middleton, SA; Wedler, FC | 1 |
Hsuanyu, YC; Kantrowitz, ER; Middleton, SA; Wedler, FC | 1 |
Kleanthous, C; Schachman, HK; Wemmer, DE | 1 |
Hsuanyu, Y; Wedler, FC | 1 |
Gouaux, JE; Krause, KL; Lipscomb, WN | 1 |
Hervé, G; Jones, PT; Moody, MF; Tauc, P; Vachette, P | 1 |
Gelbard, AS; Kaseman, DS; Meister, A; Rosenspire, KC | 1 |
Farrington, GK; Kumar, A; Wedler, FC | 1 |
Christopherson, RI; Jones, ME; Yu, ML | 1 |
Hisata, T; Tatibana, M | 1 |
Yon, RJ | 1 |
Christopherson, RI; Duggleby, RG | 1 |
Burns, CM; Chernov, MV; Ishizaka, Y; Stark, GR | 1 |
Baker, DP; Fetler, L; Kantrowitz, ER; Keiser, RT; Vachette, P | 1 |
Hu, P; Switzer, RL | 1 |
Allewell, NM; Bromberg, S; LiCata, VJ; Mallikarachchi, D | 1 |
England, P; Hervé, G; Leconte, C; Tauc, P | 1 |
Lum, L; Schachman, HK; Waldrop, GL; Zhou, BB | 1 |
Ley, BW; Moyer, ML; Wedler, FC | 1 |
Baur, H; Dideberg, O; Haas, D; Schmid, S; Stalon, V; Tricot, C; Villeret, V | 1 |
Aucoin, JM; Baker, DP; deMello, LA; Kantrowitz, ER; Williams, MK | 1 |
Burns, BP; Hazell, SL; Mendz, GL | 1 |
Chen, PG; Desmarez, L; Glansdorff, N; Legrain, C; Piérard, A; Van de Casteele, M | 1 |
Kantrowitz, ER; Tsuruta, H; Vachette, P | 1 |
Evans, D; Guy, H; Hervé, G; Lux, M; Penverne, B; Rotgeri, A; Serre, V | 1 |
Brosnan, JT; Brosnan, ME; Nissim, I; Yudkoff, M | 1 |
Carrey, EA; Fairbanks, LD; Kirschbaum, B; Rückemann, K; Simmonds, HA; Swaminathan, R | 1 |
Davidson, JN; Qiu, Y | 1 |
Huang, X; Raushel, FM | 1 |
Buttner, MJ; Molle, V | 1 |
Holden, HM; Neal, TM; Phillips, GN; Raushel, FM; Thoden, JB | 1 |
DERKS, M; GRISOLIA, S | 1 |
HAGER, SE; HERZFELD, A; JONES, ME | 1 |
THAYER, SA; TREMBLAY, GC | 1 |
Batista, Fde A; Bosch, SS; Groves, MR; Lunev, S; Wrenger, C | 1 |
56 other study(ies) available for carbamyl phosphate and aspartic acid
Article | Year |
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Evidence from 13C NMR for protonation of carbamyl-P and N-(phosphonacetyl)-L-aspartate in the active site of aspartate transcarbamylase.
Topics: Aspartic Acid; Binding Sites; Carbamates; Carbamyl Phosphate; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Organophosphonates; Protein Binding; Structure-Activity Relationship | 1976 |
Bohr effect in Escherichia coli aspartate transcarbamylase. Linkages between substrate binding, proton binding, and conformational transitions.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Calorimetry; Carbamyl Phosphate; Escherichia coli; Hydrogen-Ion Concentration; Oxyhemoglobins; Phosphonoacetic Acid; Potentiometry; Protein Conformation; Protons; Spectrophotometry; Succinates | 1979 |
A kinetic model of cooperativity in aspartate transcarbamylase.
Topics: Adenosine Triphosphate; Allosteric Regulation; Allosteric Site; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Cytosine Nucleotides; Escherichia coli; Kinetics; Ligands; Models, Biological; Phosphates; Protein Conformation; Structure-Activity Relationship; Succinates | 1977 |
Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate.
Topics: Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Escherichia coli; Kinetics; Mathematics; Molecular Weight; Protein Conformation; Ultracentrifugation | 1977 |
Calorimetric analysis of aspartate transcarbamylase from Escherichia coli. Binding of substrates and substrate analogues to the native enzyme and catalytic subunit.
Topics: Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Calorimetry; Carbamyl Phosphate; Escherichia coli; Macromolecular Substances; Phosphonoacetic Acid; Protein Conformation; Thermodynamics | 1978 |
Structure and function of aspartate transcarbamoylase studied using chymotrypsin as a probe.
Topics: Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Chymotrypsin; Escherichia coli; Kinetics; Macromolecular Substances; Protein Conformation; Structure-Activity Relationship; Succinates | 1978 |
Response of the pyrimidine pathway of Escherichia coli K 12 to exogenous adenine and uracil.
Topics: Adenine; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Carbamyl Phosphate; Escherichia coli; Kinetics; Orotate Phosphoribosyltransferase; Orotic Acid; Pyrimidines; Uracil | 1978 |
Wheat-germ aspartate transcarbamoylase. Steady-state kinetics and stereochemistry of the binding site for L-aspartate.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamates; Carbamyl Phosphate; Kinetics; Molecular Conformation; Seeds; Triticum | 1979 |
Antitumor activity of N-(phosphonacetyl)-L-aspartic acid, a transition-state inhibitor of aspartate transcarbamylase.
Topics: Animals; Antineoplastic Agents; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Drug Administration Schedule; Female; Leukemia L1210; Leukemia, Experimental; Lung Neoplasms; Male; Melanoma; Mice; Neoplasms, Experimental; Organophosphorus Compounds; Osteosarcoma; Phosphonoacetic Acid | 1976 |
Enzymatic synthesis of labeled carbamyl- aspartic acid.
Topics: Animals; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamates; Carbamyl Phosphate; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Paper; Eukaryota; Evaluation Studies as Topic; Methods | 1975 |
The role of chemical equilibria in organ function.
Topics: Alanine; Amino Acids; Ammonia; Animals; Aspartic Acid; Carbamyl Phosphate; Female; Glutamate Dehydrogenase; Glutaminase; Glutamine; Humans; Kidney; Metabolism; Rats; Thermodynamics; Transaminases; Urea | 1975 |
Regulation of aspartate carbamoyltransferase in Neisseria and Branhamella species.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Chloromercuribenzoates; Enzyme Activation; Hot Temperature; Molecular Weight; Moraxella; Neisseria; Nucleotides; p-Chloromercuribenzoic Acid | 1992 |
Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Computer Simulation; Cytidine Triphosphate; Escherichia coli; Kinetics; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Structure-Activity Relationship | 1992 |
Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase.
Topics: Amino Acids; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Carbon Radioisotopes; Catalysis; Escherichia coli; Hydrogen-Ion Concentration; Ions; Kinetics; Phosphonoacetic Acid; Recombinant Proteins | 1992 |
13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Carbon Isotopes; Cysteine; Cytidine Triphosphate; Escherichia coli; Hydrogen-Ion Concentration; In Vitro Techniques; Kinetics; Macromolecular Substances; Neurotransmitter Agents | 1992 |
The contribution of threonine 55 to catalysis in aspartate transcarbamoylase.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Base Sequence; Carbamyl Phosphate; Carbon Isotopes; Catalysis; Deuterium; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrogen Isotopes; Oligonucleotides; Phosphonoacetic Acid; Structure-Activity Relationship; Succinates; Threonine | 1992 |
Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Cytidine Triphosphate; DNA Mutational Analysis; Histidine; Lysine; Phosphonoacetic Acid; Structure-Activity Relationship | 1991 |
Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Glutamates; Glutamic Acid; Glutamine; Phosphonoacetic Acid; Protein Engineering; Structure-Activity Relationship; X-Ray Diffraction | 1990 |
Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Kinetics; Mutation; Phosphonoacetic Acid; Protein Conformation | 1990 |
The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate.
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 |
Function of threonine-55 in the carbamoyl phosphate binding site of Escherichia coli aspartate transcarbamoylase.
Topics: Alanine; Antineoplastic Agents; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Escherichia coli; Kinetics; Molecular Structure; Mutation; Phosphonoacetic Acid; Protein Conformation; Threonine | 1989 |
Site-specific mutation of Tyr240----Phe in the catalytic chain of Escherichia coli aspartate transcarbamylase. Consequences for kinetic mechanism.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Catalysis; Computer Simulation; Escherichia coli; Kinetics; Mutation; Phenylalanine; Phosphates; Protein Conformation; Structure-Activity Relationship; Thermodynamics; Tyrosine | 1989 |
Regulatory behavior of Escherichia coli aspartate transcarbamylase altered by site-specific mutation of Tyr240----Phe in the catalytic chain.
Topics: Adenosine Triphosphate; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Catalysis; Computer Simulation; Cytidine Triphosphate; Enzyme Activation; Escherichia coli; Kinetics; Mutation; Phenylalanine; Phosphates; Structure-Activity Relationship; Thermodynamics; Tyrosine | 1989 |
The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Phosphonoacetic Acid; Succinates; Succinic Acid | 1988 |
Kinetic mechanism of catalytic subunits (c3) of E. coli aspartate transcarbamylase at pH 7.0.
Topics: Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Catalysis; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances | 1988 |
The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Chemical Phenomena; Chemistry; Escherichia coli; Hydrogen Bonding; Models, Chemical; Molecular Conformation; Phosphonoacetic Acid | 1987 |
Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding.
Topics: Adenosine Triphosphate; Allosteric Site; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Macromolecular Substances; Phosphonoacetic Acid; X-Rays | 1985 |
Enzymatic syntheses of carbamyl phosphate, L-citrulline, and N-carbamyl L-aspartate labeled with either 13N or 11C.
Topics: Animals; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamates; Carbamoyl-Phosphate Synthase (Ammonia); Carbamyl Phosphate; Carbon Isotopes; Carbon Radioisotopes; Chromatography, High Pressure Liquid; Citrulline; Female; Isotope Labeling; Mice; Mice, Inbred Strains; Nitrogen Radioisotopes; Ornithine Carbamoyltransferase; Radioisotope Dilution Technique; Tissue Distribution | 1985 |
Design and synthesis of new transition-state analogue inhibitors of aspartate transcarbamylase.
Topics: Antimetabolites, Antineoplastic; Aspartate Carbamoyltransferase; Aspartic Acid; Binding, Competitive; Carbamyl Phosphate; Chemical Phenomena; Chemistry; Kinetics; Organophosphorus Compounds; Organothiophosphorus Compounds; Phosphonoacetic Acid; Structure-Activity Relationship | 1985 |
An overall radioassay for the first three reactions of de novo pyrimidine biosynthesis.
Topics: Amidohydrolases; Aspartate Carbamoyltransferase; Aspartic Acid; Bicarbonates; Carbamoyl-Phosphate Synthase (Ammonia); Carbamyl Phosphate; Carbon Radioisotopes; Clostridium; Dihydroorotase; Enterococcus faecalis; Kinetics; Ligases; Pyrimidines; Radioisotope Dilution Technique | 1981 |
Control of de novo pyrimidine biosynthesis in mammalian tissues. Levels and turnover of early intermediates in mouse spleen in vivo.
Topics: Animals; Aspartic Acid; Azauridine; Bicarbonates; Carbamates; Carbamyl Phosphate; Kinetics; Male; Mice; Orotic Acid; Phenylhydrazines; Pyrimidines; Spleen; Uridine Monophosphate | 1980 |
Regulatory kinetics of wheat-germ aspartate transcarbamoylase. Adaptation of the concerted model to account for complex kinetic effects of uridine 5'-monophosphate.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Kinetics; Models, Chemical; Phosphonoacetic Acid; Plants; Protein Conformation; Triticum; Uracil Nucleotides; Uridine Monophosphate | 1984 |
Metabolic resistance: the protection of enzymes against drugs which are tight-binding inhibitors by the accumulation of substrate.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Drug Resistance; Models, Chemical; Orotidine-5'-Phosphate Decarboxylase; Phosphonoacetic Acid | 1983 |
p53-dependent growth arrest of REF52 cells containing newly amplified DNA.
Topics: Animals; Antigens, Viral, Tumor; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cell Cycle; Cell Line; Cyclin-Dependent Kinase Inhibitor p21; Cyclins; Dihydroorotase; DNA Damage; DNA Replication; Drug Resistance; Gene Amplification; Hot Temperature; In Situ Hybridization, Fluorescence; Ligases; Mutation; Phosphonoacetic Acid; Rats; Recombinant Proteins; RNA, Messenger; Selection, Genetic; Simian virus 40; Tumor Suppressor Protein p53 | 1995 |
Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase.
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 |
Evidence for substrate stabilization in regulation of the degradation of Bacillus subtilis aspartate transcarbamylase in vivo.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Bacillus subtilis; Carbamyl Phosphate; Circular Dichroism; Enzyme Stability; Guanidine; Guanidines; Hot Temperature; Ligases; Mutation; Protein Denaturation; Recombinant Proteins; Subtilisins | 1995 |
Ligation alters the pathway of urea-induced denaturation of the catalytic trimer of Escherichia coli aspartate transcarbamylase.
Topics: Adenosine Triphosphate; Anions; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Catalysis; Chemical Phenomena; Chemistry, Physical; Chlorides; Escherichia coli; Macromolecular Substances; Phosphonoacetic Acid; Protein Denaturation; Protein Folding; Spectrophotometry; Thermodynamics; Urea | 1994 |
Apparent cooperativity for carbamoylphosphate in Escherichia coli aspartate transcarbamoylase only reflects cooperativity for aspartate.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Dialysis; Escherichia coli; Substrate Specificity; Succinates; Succinic Acid | 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.
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 |
A continuous visible spectrophotometric assay for aspartate transcarbamylase.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Kinetics; Microchemistry; Sensitivity and Specificity; Spectrophotometry | 1994 |
Catabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa. Changes of allosteric properties resulting from modifications at the C-terminus.
Topics: Adenosine Monophosphate; Allosteric Regulation; Amino Acid Sequence; Aspartic Acid; Base Sequence; Carbamyl Phosphate; Catalysis; Citrulline; Hydrogen-Ion Concentration; Isoleucine; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Ornithine Carbamoyltransferase; Pseudomonas aeruginosa; Spermidine; Structure-Activity Relationship | 1994 |
Overexpression and purification of the trimeric aspartate transcarbamoylase from Bacillus subtilis.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Bacillus subtilis; Carbamyl Phosphate; Chromatography; Cloning, Molecular; Escherichia coli; Kinetics; Plasmids; Recombinant Proteins | 1995 |
In situ properties of Helicobacter pylori aspartate carbamoyltransferase.
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 |
Molecular physiology of carbamoylation under extreme conditions: what can we learn from extreme thermophilic microorganisms?
Topics: Archaea; Aspartate Carbamoyltransferase; Aspartic Acid; Bacteria; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Carbamyl Phosphate; Citrulline; Dihydroorotase; Enzyme Stability; Genes, Bacterial; Hot Temperature; Ornithine Carbamoyltransferase; Thermodynamics; Thermus | 1997 |
Direct observation of an altered quaternary-structure transition in a mutant aspartate transcarbamoylase.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Bacterial Proteins; Carbamyl Phosphate; Escherichia coli; Models, Molecular; Point Mutation; Protein Conformation; Substrate Specificity; X-Ray Diffraction | 1998 |
Half of Saccharomyces cerevisiae carbamoyl phosphate synthetase produces and channels carbamoyl phosphate to the fused aspartate transcarbamoylase domain.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Carbamyl Phosphate; Feedback; Multienzyme Complexes; Phosphonoacetic Acid; Phosphotransferases (Carboxyl Group Acceptor); Plasmids; Pyrimidines; Saccharomyces cerevisiae; Uridine Triphosphate | 1999 |
Studies of hepatic glutamine metabolism in the perfused rat liver with (15)N-labeled glutamine.
Topics: Ammonia; Animals; Aspartic Acid; Carbamyl Phosphate; Citrulline; Glucagon; Glutamates; Glutaminase; Glutamine; Insulin; Liver; Male; Nitrogen Isotopes; Oxygen Consumption; Perfusion; Rats; Rats, Sprague-Dawley; Urea | 1999 |
Simultaneous separation by high-performance liquid chromatography of carbamoyl aspartate, carbamoyl phosphate and dihydroorotic acid.
Topics: Anti-Inflammatory Agents, Non-Steroidal; Aspartic Acid; Biphenyl Compounds; Carbamyl Phosphate; Chromatography, High Pressure Liquid; Humans; Immunosuppressive Agents; Isoxazoles; Leflunomide; Orotic Acid; T-Lymphocytes | 1999 |
Substitutions in the aspartate transcarbamoylase domain of hamster CAD disrupt oligomeric structure.
Topics: Animals; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Carbamyl Phosphate; CHO Cells; Cricetinae; Dihydroorotase; Encephalomyocarditis virus; Molecular Structure; Multienzyme Complexes; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Plasmids; Protein Conformation; Transfection | 2000 |
An engineered blockage within the ammonia tunnel of carbamoyl phosphate synthetase prevents the use of glutamine as a substrate but not ammonia.
Topics: Alanine; Ammonia; Aspartic Acid; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Carbamyl Phosphate; Escherichia coli; Glutamic Acid; Glutamine; Glycine; Kinetics; Lysine; Methionine; Mutagenesis, Site-Directed; Phenylalanine; Serine; Substrate Specificity; Time Factors | 2000 |
Different alleles of the response regulator gene bldM arrest Streptomyces coelicolor development at distinct stages.
Topics: Alleles; Amino Acid Sequence; Aspartic Acid; Bacterial Proteins; Base Sequence; Carbamyl Phosphate; DNA-Binding Proteins; DNA, Bacterial; Genes, Bacterial; Helix-Turn-Helix Motifs; Methylnitronitrosoguanidine; Molecular Sequence Data; Mutagenesis; Organophosphates; Phosphorylation; Response Elements; Streptomyces; Transcription Factors | 2000 |
Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center.
Topics: Amino Acid Sequence; Aryldialkylphosphatase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Catalysis; Crystallography, X-Ray; Dihydroorotase; Dimerization; Escherichia coli; Esterases; Humans; Lysine; Molecular Sequence Data; Orotic Acid; Structure-Activity Relationship; Zinc | 2001 |
Biosynthesis of a metabolically active citrulline-like material unrelated to carbamyl aspartate and carbamyl phosphate.
Topics: Amino Acids; Aspartic Acid; Carbamyl Phosphate; Citrulline; Humans; Liver | 1958 |
THE CARBAMYL PHOSPHATE CONTENT OF RABBIT BLOOD PLASMA.
Topics: Aspartic Acid; Blood Chemical Analysis; Carbamates; Carbamyl Phosphate; Esters; Phosphates; Pyrimidines; Rabbits; Research; Transferases | 1964 |
THE EFFECT OF ESTRADIOL-17-BETA ON THE ACTIVITY OF CARBAMOYL PHOSPHATE:L-ASPARTATE CARBAMOYL TRANSFERASE IN THE UTERI OF IMMATURE RATS.
Topics: Aspartic Acid; Carbamyl Phosphate; Carbon Isotopes; Carboxyl and Carbamoyl Transferases; Dactinomycin; DNA; Estradiol; Female; Humans; Metabolism; Pharmacology; Puromycin; Rats; Research; RNA; Transferases; Uterus | 1964 |
Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum.
Topics: Amino Acid Sequence; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Catalytic Domain; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli; Gene Expression; Kinetics; Models, Molecular; Mutation; Plasmids; Plasmodium falciparum; Protein Binding; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Structure, Secondary; Protozoan Proteins; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity | 2016 |