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Functional comparison of the two Bacillus anthracis glutamate racemases
Dylan Dodd
, Joseph G. Reese
, Craig R. Louer
, Jimmy D. Ballard
, M. Ashley Spies
,
Steven R. Blanke
Microbiology
Pathobiology
Biomedical and Translational Sciences
Center for Global Studies
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peer-review
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Keyphrases
Bacillus Anthracis
100%
Glutamate Racemase
100%
Functional Comparison
100%
L-glutamine
83%
Stereoisomerization
50%
Binding Residues
33%
Site-directed mutagenesis
16%
Active Sites
16%
Size Exclusion Chromatography
16%
Recombinant
16%
High-order
16%
Escherichia Coli
16%
Genome Sequencing
16%
PH Dependence
16%
Attenuation
16%
Enzymatic Activity
16%
Kinetic Properties
16%
Steady-state Kinetics
16%
Drug Design
16%
Homology Modeling
16%
Active Pocket
16%
Recombinant Protein
16%
Quaternary Structure
16%
Site Features
16%
Virulence
16%
Anthracis
16%
Pharmacophore
16%
Peptidoglycan Synthesis
16%
Capsule Biosynthesis
16%
Titratable
16%
Biochemistry, Genetics and Molecular Biology
Bacillus Anthracis
100%
Glutamic Acid
100%
Active Site
36%
Mutagenesis
9%
Anabolism
9%
Steady State
9%
Escherichia coli
9%
Enzyme Activity
9%
Homology Modeling
9%
Potential Difference
9%
Size-Exclusion Chromatography
9%
Recombinant Protein
9%
Protein Quaternary Structure
9%
Pharmacophore
9%
Genomics
9%
Peptidoglycan
9%