Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase

Keyphrases

• Chloride 100%
• O-acetylserine Sulfhydrylase 100%
• Anion Binding Site 100%
• External Aldimine 42%
• Allosteric Site 42%
• PH Range 28%
• Sulfide 28%
• Active Sites 14%
• Dimer Interface 14%
• Side Chain 14%
• Spectral Studies 14%
• Steady State 14%
• Methionine 14%
• Cysteine 14%
• Isozymes 14%
• Kinetic Study 14%
• Physiologic 14%
• Steady-state Kinetics 14%
• UV-visible 14%
• Dissociation Constant 14%
• New Crystal Structures 14%
• PH-independent 14%
• Internal Aldimine 14%
• O-Acetyl-L-serine 14%
• 2-aminoacrylate 14%
• Norleucine 14%
• Aldimines 14%
• Ionizable 14%

Biochemistry, Genetics and Molecular Biology

• Binding Site 100%
• Serine 100%
• Sulfate 100%
• Allosteric Site 100%
• Enzyme 33%
• Active Site 33%
• Cysteine 33%
• Crystal Structure 33%
• Isozyme 33%
• Steady State 33%
• Methionine 33%
• Dissociation Constant 33%
• Presteady-State Kinetics 33%

Pharmacology, Toxicology and Pharmaceutical Science

• Serine 100%
• Sulfate 100%
• Binding Site 100%
• Anion 100%
• Methionine 33%
• Cysteine 33%
• Isoenzyme 33%
• Dimer 33%
• Acetic Acid Derivative 33%
• Norleucine 33%