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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2015, Volume 112, Issue 36, pp. 11247 - 11251
Computational chemistry predicts that atomic motions on the femtosecond timescale are coupled to transition-state formation (barrier-crossing) in human purine... 
Heavy enzymes | Transition state coupling | Born-Oppenheimer enzymes | Femtosecond dynamics | Pre-steady-state chemistry | femtosecond dynamics | SITE | pre-steady-state chemistry | MULTIDISCIPLINARY SCIENCES | transition state coupling | TRANSITION-STATE | ENZYMATIC-REACTION | MOTIONS | PROMOTING VIBRATIONS | heavy enzymes | PROTEIN DYNAMICS | PNP | DIHYDROFOLATE-REDUCTASE | CATALYTIC MECHANISM | Models, Chemical | Humans | Amino Acids - chemistry | Molecular Sequence Data | Chromatography, High Pressure Liquid | Histidine - metabolism | Amino Acids - genetics | Purine-Nucleoside Phosphorylase - genetics | Amino Acids - metabolism | Isotopes - chemistry | Tandem Mass Spectrometry | Ribosemonophosphates - chemistry | Guanosine - chemistry | Isotope Labeling | Purine-Nucleoside Phosphorylase - metabolism | Carbon Isotopes - chemistry | Amino Acid Sequence | Motion | Catalytic Domain | Biocatalysis | Deuterium - chemistry | Histidine - genetics | Models, Molecular | Binding Sites - genetics | Guanosine - metabolism | Nitrogen Isotopes - chemistry | Purine-Nucleoside Phosphorylase - chemistry | Kinetics | Histidine - chemistry | Ribosemonophosphates - metabolism | Physiological aspects | Amino acids | Purine nucleotides | Research | Phosphorylase | Biological Sciences | Born–Oppenheimer enzymes | pre–steady-state chemistry
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2015, Volume 290, Issue 9, pp. 5226 - 5239
Journal Article
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2012, Volume 109, Issue 16, pp. 6024 - 6029
Journal Article
Journal Article
Acta Crystallographica Section F, ISSN 2053-230X, 06/2017, Volume 73, Issue 6, pp. 369 - 375
Phosphoribosylpyrophosphate synthetase (PRPPS) from the thermophilic bacterial strain Thermus thermophilus HB27 catalyzes the synthesis of... 
microgravity | transferases | PRPP synthetase | Thermus thermophilus HB27 | phosphoribosylpyrophosphate synthetase | Protein Multimerization | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Adenosine Diphosphate - chemistry | Protein Subunits - metabolism | Ribosemonophosphates - chemistry | Adenosine Triphosphate - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Protein Subunits - genetics | Recombinant Proteins - metabolism | Ribose-Phosphate Pyrophosphokinase - chemistry | Amino Acid Sequence | Protein Conformation, alpha-Helical | Thermus thermophilus - enzymology | Catalytic Domain | Gene Expression | Thermus thermophilus - chemistry | Genetic Vectors - chemistry | Ribose-Phosphate Pyrophosphokinase - metabolism | Bacterial Proteins - genetics | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Ribose-Phosphate Pyrophosphokinase - genetics | Allosteric Site | Protein Binding | Bacterial Proteins - metabolism | Protein Subunits - chemistry | Adenosine Diphosphate - metabolism | Adenosine Triphosphate - chemistry | Ribosemonophosphates - metabolism | Binding | Crystal growth | Residues | Enzymes | Crystals | Ions | ADP | Density | Allosteric properties | Ribose | Phosphate | Bacteria | Magnesium | Catalysis | Sulfate | Chemical synthesis | Microgravity | ATP | Binding sites | Crystal structure | Recombinant
Journal Article
Acta Crystallographica Section F, ISSN 2053-230X, 11/2016, Volume 72, Issue 11, pp. 804 - 812
A phosphoribosyl anthranilate isomerase, TkTrpF, from Thermococcus kodakaraensis was expressed in Escherichia coli and purified to homogeneity. TkTrpF was... 
Thermococcus kodakaraensis | tryptophan biosynthesis | phosphoribosyl anthranilate isomerase | hyperthermophilic archaea | TIM barrel | Pyrococcus furiosus | protein stability | SYSTEM | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BIOCHEMICAL RESEARCH METHODS | PHOSPHATE SYNTHASE | MECHANISMS | CRYSTALLOGRAPHY | BIOPHYSICS | TEMPERATURE | ENZYMES | BIOSYNTHESIS | X-RAY | THERMOTOGA-MARITIMA | Pyrococcus furiosus - chemistry | ortho-Aminobenzoates - chemistry | Archaeal Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Ribosemonophosphates - chemistry | Thermococcus - enzymology | Cloning, Molecular | Escherichia coli - metabolism | Archaeal Proteins - genetics | Aldose-Ketose Isomerases - metabolism | Pyrococcus furiosus - enzymology | Archaeal Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Aldose-Ketose Isomerases - chemistry | Catalytic Domain | Gene Expression | Thermococcus - chemistry | Enzyme Stability | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Static Electricity | Plasmids - metabolism | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Plasmids - chemistry | Protein Binding | Aldose-Ketose Isomerases - genetics | ortho-Aminobenzoates - metabolism | Ribosemonophosphates - metabolism | Residues | Asymmetry | Similarity | Escherichia coli | Homogeneity | Biology | Monomers | Crystal structure
Journal Article
PLoS ONE, ISSN 1932-6203, 12/2016, Volume 11, Issue 12, p. e0167580
5'-nucleotidases (EC 3.1.3.5) catalyze the hydrolytic dephosphorylation of 5'-ribonucleotides and 5'-deoxyribonucleotides as well as complex nucleotides, such... 
NUCLEOTIDE | USHA | REGULATOR | CYTOPLASMIC 5'-NUCLEOTIDASES | GENERAL ENZYMATIC SCREENS | PHOSPHATASE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | SEQUENCE | DEHALOGENASE SUPERFAMILY | PROTEINS | 5'-Nucleotidase - genetics | Ribonucleotides - metabolism | Ribonucleotides - chemistry | Substrate Specificity | Bacillus subtilis - enzymology | Recombinant Proteins - genetics | Bacillus subtilis - chemistry | Recombinant Proteins - biosynthesis | Bacillus subtilis - genetics | Hydrolysis | Ribosemonophosphates - chemistry | Escherichia coli - genetics | 5'-Nucleotidase - chemistry | Kinetics | Gene Expression Regulation, Bacterial | Ribosemonophosphates - metabolism | 5'-Nucleotidase - biosynthesis | Physiological aspects | Genetic aspects | Research | Gene expression | Bacillus subtilis | Nucleotidases | NADPH | Phosphates | Transcription | Amino acids | Nucleotides | Dephosphorylation | Glucose | Kinases | Phosphatase | Proteins | Signal transduction | Deoxyribonucleotides | E coli | Ribose | Substrate specificity | Bacteria | Catalysis | Bioinformatics | Deoxyribonucleic acid--DNA | Recombinant | Enzymes | 5'-Nucleotidase | Phosphohydrolase | Cloning | Metabolism | Carbon | Substrates | Flavin-adenine dinucleotide | NAD | Ribonucleotides | p-Nitrophenyl | Plasmids | Nicotinamide adenine dinucleotide | Uridine | Nucleosides | Regulation | Nicotinamide | Polyhistidine | Deoxyribonucleic acid | DNA
Journal Article