V_max regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase

Keyphrases

• Vmax 100%
• Glyceraldehyde-3-phosphate Dehydrogenase 100%
• Active Form 100%
• Conformational Change 66%
• α-ketoglutarate (α-KG) 66%
• Nucleotide Binding 66%
• Escherichia Coli 33%
• Signal Transduction 33%
• Inhibitory Signaling 33%
• Nicotinamide Adenine Dinucleotide (NAD+) 33%
• CRISTAL 33%
• Redox Reaction 33%
• Catalytic Reaction 33%
• X-ray Crystallography 33%
• Active Sites 33%
• Catalytic Site 33%
• Cooperative Effects 33%
• X-ray Crystal Structure 33%
• Sulfate Anion 33%
• Homotetramer 33%
• Active Conformation 33%
• Phosphate Anion 33%
• Coordinated Movement 33%
• Crystal Conformation 33%
• Active Site Cleft 33%
• Nonphysiological 33%

Biochemistry, Genetics and Molecular Biology

• Conformation 100%
• Maximum Reaction Velocity 100%
• Phosphoglycerate Dehydrogenase 100%
• Serine 100%
• Active Site 66%
• Crystal Structure 66%
• Conformational Change 66%
• Nucleotide 66%
• X Ray 33%
• Signal Transduction 33%
• Sulfate 33%
• X-Ray Crystallography 33%
• Oxidation Reduction Reaction 33%
• Coenzyme NAD 33%
• Homotetramer 33%
• Escherichia coli 33%
• Crystal 33%