Functional role of the conserved active site proline of triosephosphate isomerase

Keyphrases

• 2,3-diphosphoglycerate 50%
• Active Loop 16%
• Active Sites 100%
• Carboxylic Acid Moiety 16%
• Catalytic Residues 16%
• Conformational Change 33%
• Crystalline Properties 16%
• Enzymatic Properties 16%
• Functional Role 100%
• In the Wild 16%
• Km Value 16%
• Ligand Binding 33%
• Peptide Plane 16%
• Phosphate 33%
• Proline 100%
• Reaction Mechanism 16%
• Side Chain 50%
• Structural Comparison 16%
• Transition State Analogue 16%
• Triosephosphate Isomerase 100%
• Turnover number 16%
• Unique Properties 16%

INIS

• affinity 16%
• analog states 16%
• carboxylic acids 16%
• chains 50%
• comparative evaluations 16%
• conformational changes 33%
• crystal structure 16%
• crystallography 16%
• enzymes 16%
• interactions 33%
• isomerases 100%
• ligands 33%
• mutants 16%
• peptides 16%
• phosphates 33%
• proline 100%
• reaction mechanisms 16%
• residues 16%
• rotation 16%
• substrates 16%
• values 16%

Biochemistry, Genetics and Molecular Biology

• Active Site 100%
• Conformation 16%
• Conformational Change 33%
• Crystal Structure 16%
• Enzyme 16%
• Ligand Binding 33%
• Proline 100%
• Transition State Analog 16%
• Triosephosphate Isomerase 100%
• Turnover Number 16%
• Wild Type 50%