Biochemical analysis of escherichia coli selenophosphate synthetase mutants: Lysine 20 is essential for catalytic activity and cysteine 17/19 for 8-azido-ATP derivatization

Keyphrases

• Escherichia Coli 100%
• Catalytic Activity 100%
• Cysteine 100%
• Biochemical Analysis 100%
• Selenophosphate Synthetase 100%
• Lysine 100%
• Derivatization 100%
• Azido 100%
• Mutant Enzyme 66%
• ATP Binding 66%
• Km Value 33%
• N-terminus 33%
• Fold Increase 33%
• Peptide Sequencing 33%
• Selenide 33%
• Binding Properties 33%
• Cysteine Residues 33%
• Glycine-rich 33%
• Gel Filtration 33%
• GTP Binding 33%
• Site-directed mutagenesis 33%
• Vmax 33%
• Selenium Donor 33%
• Selenophosphate 33%
• 4-fold 33%
• ATP Analogues 33%
• ATP Binding Site 33%
• Photoaffinity Labeling 33%

Biochemistry, Genetics and Molecular Biology

• Escherichia coli 100%
• Adenosine Triphosphate 100%
• Biochemical Analysis 100%
• Derivatization 100%
• Enzymatic Activity 100%
• Cysteine 100%
• Lysine 100%
• Enzyme 36%
• Arginine 18%
• Wild Type 9%
• N-Terminus 9%
• Binding Site 9%
• Peptide Sequence 9%
• Guanosine Triphosphate 9%
• Gel Filtration 9%
• Site-Directed Mutagenesis 9%
• Maximum Reaction Velocity 9%
• Photoaffinity Labeling 9%
• Serine 9%
• Selenide 9%

Pharmacology, Toxicology and Pharmaceutical Science

• Selenide 9%