Evolution of homo-oligomerization of methionine S-adenosyltransferases is replete with structure–function constrains

Keyphrases

• Structure Function 100%
• Co-oligomerization 100%
• S-adenosylmethionine Decarboxylase 100%
• Homomeric 42%
• Neisseria Gonorrhoeae 28%
• Homotetramer 28%
• Functional Regulation 28%
• Physicochemical Properties 14%
• Molecular Mechanism 14%
• Escherichia Coli 14%
• Structural Integrity 14%
• Active Sites 14%
• Hydrophobic Interaction 14%
• Electrostatic Interaction 14%
• High Flexibility 14%
• Hydrophobicity 14%
• Methionine 14%
• Protein-protein Interface 14%
• Evolutionary Change 14%
• Quaternary Complex 14%
• Metabolic Enzymes 14%
• Kinetic Stability 14%
• Dimer Interface 14%
• Complex Assembly 14%
• Structure Evolution 14%
• Quaternary Structure 14%
• Evolutionary Variation 14%
• Substrate-induced 14%
• Kinetically Stable 14%
• Active Loop 14%
• Dimer Assembly 14%
• Interface Integrity 14%
• Induced Assembly 14%
• Homomerization 14%
• Bacterial Proteome 14%
• Homomer 14%

Biochemistry, Genetics and Molecular Biology

• Oligomerization 100%
• Methionine 100%
• Enzyme 25%
• Active Site 25%
• Neisseria gonorrhoeae 25%
• Homotetramer 25%
• Adenosine Triphosphate 12%
• Static Electricity 12%
• Proteome 12%
• Escherichia coli 12%
• Hydrophobicity 12%
• Protein Quaternary Structure 12%