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Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2014, Volume 111, Issue 23, pp. 8535 - 8540
The rate of protein evolution is determined by a combination of selective pressure on protein function and biophysical constraints on protein folding and... 
Proteins | Enzymes | Active sites | Divergent evolution | Evolution | Amino acids | Biochemistry | Monomers | Family members | Family structure | Protein structure | Protein structure-function relationships | Enolase superfamily | ACTIVE-SITE | MULTIDISCIPLINARY SCIENCES | ENZYMATIC-ACTIVITIES | ESCHERICHIA-COLI | ACYLAMINO ACID RACEMASE | protein structure | O-SUCCINYLBENZOATE SYNTHASE | MANDELATE RACEMASE | UNIVERSAL DISTRIBUTION | enolase superfamily | DOMAIN SUPERFAMILIES | HIGHLY EXPRESSED PROTEINS | protein structure-function relationships | Bacterial Proteins - chemistry | Crystallography, X-Ray | Phylogeny | INDEL Mutation | Carbon-Carbon Lyases - genetics | Deinococcus - genetics | Genetic Variation | Thermus thermophilus - genetics | Protein Structure, Quaternary | Carbon-Carbon Lyases - chemistry | Deinococcus - enzymology | Enterococcus faecalis - enzymology | Listeria - genetics | Protein Structure, Tertiary | Thermus thermophilus - enzymology | Catalytic Domain | Protein Structure, Secondary | Enterococcus faecalis - genetics | Bacterial Proteins - genetics | Carbon-Carbon Lyases - classification | Models, Molecular | Bacteria - genetics | Bacteria - enzymology | Bacterial Proteins - classification | Listeria - enzymology | Evolution, Molecular | Protein research | Research | Nucleotide sequencing | Structure | DNA sequencing | Biological Sciences
Journal Article
Journal Article
The FEBS Journal, ISSN 1742-464X, 03/2013, Volume 280, Issue 6, pp. 1475 - 1490
Thermostable nucleoside phosphorylases are attractive biocatalysts for the synthesis of modified nucleosides. Hence we report on the recombinant expression of... 
2′–deoxyfluoro adenine nucleosides | thermostable PNP | Aeropyrum pernix | Geobacillus thermoglucosidasius | Deinococcus geothermalis | Deinococcus geothermalis | Geobacillus thermoglucosidasius | Aeropyrum pernix | 2′-deoxyfluoro adenine nucleosides | 2 '-deoxyfluoro adenine nucleosides | BIOCHEMISTRY & MOLECULAR BIOLOGY | SULFOLOBUS-SOLFATARICUS | Aeropyrumpernix | ENZYMATIC-SYNTHESIS | Geobacillusthermoglucosidasius | OLIGONUCLEOTIDES | SUBSTRATE-SPECIFICITY | GENE | STRUCTURAL BASIS | 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE | SP-NOV | Deinococcusgeothermalis | CONFORMATIONAL-ANALYSIS | EFFICIENT | Phosphorylation | Temperature | Molecular Sequence Data | Substrate Specificity | Geobacillus - enzymology | Purine-Nucleoside Phosphorylase - genetics | Deinococcus - genetics | Cloning, Molecular | Escherichia coli - metabolism | Deinococcus - enzymology | Purine-Nucleoside Phosphorylase - metabolism | Aeropyrum - genetics | Geobacillus - genetics | Purine Nucleosides - metabolism | Pyrimidine Nucleosides - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Purine-Nucleoside Phosphorylase - isolation & purification | Enzyme Stability | Solubility | Enzyme Assays | Glycosylation | Recombinant Proteins - genetics | Deoxyadenosines - metabolism | Sequence Alignment | DNA, Bacterial - genetics | Escherichia coli - genetics | Aeropyrum - enzymology | Enzyme Activation | Kinetics | Nucleosides | Enzymes | Heterocyclic compounds | Analysis | Biosynthesis | Protein synthesis
Journal Article
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 12/2015, Volume 587, pp. 18 - 30
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 12/2016, Volume 84, Issue 12, pp. 1810 - 1822
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 11/2010, Volume 403, Issue 4, pp. 578 - 590
UDP (uridine di. phosphate) galactopyranose mutase (UGM) is involved in the cell wall biosynthesis of many pathogenic microorganisms. UGM catalyzes the... 
Enzyme inhibition and binding | Phosphonate analog | UDP-galactopyranose mutase | SPECIFICITY | ENZYME-CATALYZED SYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | GALACTOFURANOSE | GLCNAC TRANSFERASE | CRYSTAL-STRUCTURES | enzyme inhibition and binding | SUBSTRATE-ANALOGS | SUGAR NUCLEOTIDES | PURIFICATION | phosphonate analog | CHEMICAL-SYNTHESIS | BINDING | Nucleotidyltransferases - chemistry | Galactose - pharmacology | Uridine Diphosphate - analogs & derivatives | Crystallography, X-Ray | Molecular Probes - pharmacology | Deinococcus - genetics | Galactose - analogs & derivatives | Klebsiella pneumoniae - genetics | Deinococcus - enzymology | Intramolecular Transferases - chemistry | Uridine Diphosphate - pharmacology | Arabidopsis Proteins - genetics | Catalytic Domain | Recombinant Proteins - antagonists & inhibitors | Intramolecular Transferases - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Uridine Diphosphate - chemistry | Molecular Probes - chemical synthesis | Uridine Diphosphate - chemical synthesis | Galactose - chemical synthesis | Galactose - chemistry | Molecular Probes - chemistry | Arabidopsis Proteins - chemistry | Intramolecular Transferases - antagonists & inhibitors | Mycobacterium tuberculosis - enzymology | Klebsiella pneumoniae - enzymology | Nucleotidyltransferases - genetics | Protein Conformation | Mycobacterium tuberculosis - genetics | Enzymes | Pneumonia | Bacterial pneumonia | Phosphonates | Crystals | Arabidopsis thaliana | Enzyme inhibitors | Tuberculosis | Ionization | Analysis | Physiological aspects | Structure | Mass spectrometry
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2015, Volume 290, Issue 19, pp. 11948 - 11968
Journal Article