Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and Triton

Keyphrases

• Active Sites 75%
• Amino Acid Residues 50%
• Apoenzyme 25%
• Binding Site 25%
• Catalytic Loop 25%
• Catalytic Mechanism 100%
• Catalytic Role 25%
• Chain Elongation 25%
• Chain Length 25%
• Chelates 25%
• Condensation 25%
• Double mutation 25%
• Enzyme Activity 25%
• Escherichia Coli 50%
• Farnesyl Pyrophosphate 50%
• High Concentration 25%
• Hydrocarbons 25%
• Isopentenyl Pyrophosphate 100%
• Kinetic Analysis 25%
• Km Value 25%
• Magnesium Ion 25%
• Metal Ions 25%
• Mg2+ 25%
• Pyrophosphate 25%
• Robinson 25%
• Site-directed mutation 25%
• Sulfate Ion 50%
• Sulfate Magnesium 100%
• Triton 100%
• Triton X-100 (TX-100) 25%
• Undecaprenyl Pyrophosphate 50%
• Undecaprenyl Pyrophosphate Synthase 100%

Biochemistry, Genetics and Molecular Biology

• Active Site 60%
• Alanine 20%
• Amino Acids 40%
• Binding Site 20%
• Catalytic Mechanism 100%
• Crystal Structure 100%
• Enzyme Activity 20%
• Escherichia coli 40%
• Farnesyl Pyrophosphate 40%
• Isopentenyl Pyrophosphate 80%
• Kinetics 20%
• Magnesium Sulfate 100%
• Pyrophosphate 100%
• Sulfate 40%
• Synthase 100%