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bacillaceae - enzymology (241) 241
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BMC Genomics, ISSN 1471-2164, 2012, Volume 13, Issue 1, pp. 191 - 191
BACKGROUND: The assimilation of nitrogen in bacteria is achieved through only a few metabolic conversions between alpha-ketoglutarate, glutamate and glutamine.... 
STREPTOCOCCUS-MUTANS | LACTOBACILLUS-PLANTARUM | SUBTILIS UREABC OPERON | ASPARAGINE SYNTHETASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ESCHERICHIA-COLI | GENETICS & HEREDITY | REDUCTASE/2,3-BUTANEDIOL DEHYDROGENASE | GLUTAMINE-SYNTHETASE GENE | TRANSCRIPTION FACTOR TNRA | NUCLEOTIDE-SEQUENCE | LACTOCOCCUS-LACTIS | Bacillaceae - genetics | Lactobacillaceae - genetics | Bacillaceae - enzymology | Molecular Sequence Data | Streptococcaceae - genetics | Leuconostocaceae - enzymology | Streptococcaceae - enzymology | Staphylococcaceae - genetics | Binding Sites | Glutamate-Ammonia Ligase - metabolism | Repressor Proteins - metabolism | Listeria - genetics | Amino Acid Sequence | Genome, Bacterial | Nitrogen - metabolism | Lactobacillaceae - enzymology | Ammonia - metabolism | Bacterial Proteins - genetics | Repressor Proteins - genetics | DNA - metabolism | Staphylococcaceae - enzymology | Leuconostocaceae - genetics | Glutamate-Ammonia Ligase - genetics | Bacterial Proteins - metabolism | Bacillaceae - classification | Gene Expression Regulation, Bacterial | Listeria - enzymology | Ammonia | Nitrogen metabolism | Physiological aspects | Bacillus (Bacteria) | Genetic aspects | Glutamine synthetase | Research | Ligases | Analysis | Genomics | Bacteria | Genomes | Glutamate | Chromosomes | Glutamine | Proteins | Enzymes | Metabolism | Bacteriology | reductase/2,3-butanediol dehydrogenase | glutamine-synthetase gene | lactococcus-lactis | lactobacillus-plantarum | streptococcus-mutans | nucleotide-sequence | escherichia-coli | asparagine synthetase | subtilis ureabc operon | transcription factor tnra
Journal Article
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 09/2012, Volume 114, Issue 3, pp. 251 - 256
Journal Article
Transplantation, ISSN 0041-1337, 04/2012, Volume 93, Issue 7, pp. 693 - 702
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 01/2017, Volume 12, Issue 1, p. e0169540
A novel microbial esterase, EaEST, from a psychrophilic bacterium Exiguobacterium antarcticum B7, was identified and characterized. To our knowledge, this is... 
PSYCHROPHILIC ENZYMES | ACID | PROMISCUITY | MULTIDISCIPLINARY SCIENCES | PURIFICATION | CLASSIFICATION | CARBOXYLESTERASES | COLD | SALT-TOLERANT ESTERASE | HYDROLASE | BIOCATALYSIS | Enzymes, Immobilized - metabolism | Bacillaceae - chemistry | Stereoisomerism | Nitrophenols - metabolism | Bacterial Proteins - chemistry | Bacillaceae - enzymology | Substrate Specificity | Crystallography, X-Ray | Nitrophenols - chemistry | Thermodynamics | Cloning, Molecular | Escherichia coli - metabolism | Peracetic Acid - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Enzymes, Immobilized - chemistry | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Biocatalysis | Esterases - chemistry | Bacterial Proteins - genetics | Enzyme Stability | Esterases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Hot Temperature | Esterases - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Enzymes, Immobilized - genetics | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Bacterial Proteins - metabolism | Peracetic Acid - metabolism | Kinetics | Mutation | Crystals | Bacillus (Bacteria) | Esterases | Genetic aspects | Properties | Structure | Observations | Structure-activity relationships (Biochemistry) | Enzymes | Cold | Hydrolase | Incubation | Genomics | Science | Esters | Industrial applications | Biocatalysts | Enantiomers | B7 antigen | Substrates | Proteins | Microorganisms | Biofilms | p-Nitrophenyl | Esterase | Catalysis | Acetic acid | Sedimentation & deposition | Crystal structure | Structural analysis
Journal Article
PLoS ONE, ISSN 1932-6203, 04/2017, Volume 12, Issue 4, p. e0175004
Journal Article