Characterization and engineering of thermophilic aldolases : synthesizing nitrogen-heterocycles in biosynthetic routes

Biochemistry, Genetics and Molecular Biology

• Aldolase 100%
• Fructose-Bisphosphate Aldolase 100%
• Enzyme 85%
• Synthase 28%
• Glyceraldehyde 28%
• Escherichia coli 28%
• Enzyme Specificity 28%
• Amino Acids 14%
• Anabolism 14%
• Active Site 14%
• Stereoisomerism 14%
• Enantiomer 14%
• Biocatalysis 14%
• Stereoselectivity 14%
• Stereospecificity 14%
• Binding Site 14%
• Extremophile 14%
• Sulfolobus 14%
• Thermoanaerobacter 14%

Chemistry

• Heterocyclic Compound 100%
• Aldehyde 100%
• Pyruvate 50%
• Substrate Specificity 33%
• Glyceraldehyde 33%
• Carbon Atom 16%
• Chemistry 16%
• Stereoselectivity 16%
• Stereoisomer 16%
• Condensation Reaction 16%
• 4-Hydroxyproline 16%
• Binding Site 16%
• Amino Acid 16%
• Enantiomer 16%

Pharmacology, Toxicology and Pharmaceutical Science

• Fructose Bisphosphate Aldolase 100%
• Aldehyde 54%
• Pyruvic Acid 27%
• Substrate Specificity 18%
• Glyceraldehyde 18%
• Escherichia coli 18%
• Synthetase 18%
• Carbon-Carbon Bond 9%
• Amino Acid 9%
• Hydroxyproline 9%
• Sulfolobus 9%
• Extremophile 9%
• Acetylsalicylic Acid 9%
• Binding Site 9%
• Thermoanaerobacter 9%