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Results 1 - 10 of 11 > >>
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97dimer 2 * 27000, I-site mutant A134V, sedimentation equilibrium centrifugation of diluted enzyme solution 95603
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97dimer 2 * 28098, electrospray mass spectrometry 95594
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97dimer active also as a monomer stabilized by chemical cross-linking 95592
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97dimer dimeric form is necessary to activate the enzyme because of an induced stabilization of the oxyanion hole 653855
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97dimer dimerization is required for catalytic activity, appropriate dimer formation may be required to indirectly stabilize the protease oxyanion hole revealing a novel mechanism for dimerization to regulate enzyme activity 653320
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97dimer the active two-chain assemblin can be formed from the independently cloned and expressed subunits An and Ac 95597
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97dimer the catalytically active dimer is significantly dissociated above 25°C 95600
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97dimer the enzyme exists in a monomer/dimer equilibrium in solution, but only the dimer form is catalytically active. The stability of the dimer is affected by the presence of anti-chaotrophic agents 650245
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97homodimer crystallography 681048
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97monomer SDS-PAGE 95610
Results 1 - 10 of 11 > >>