EC Number |
Subunits |
Reference |
---|
3.4.22.69 | ? |
x * 37400, SDS-PAGE, recombinant protein |
764084 |
3.4.22.69 | dimer |
a mixture of monomer and dimer at a protein concentration of 4 mg/ml and mostly monomer at 0.2 mg/ml. The dimer may be the biological functional form of the protein |
691145 |
3.4.22.69 | dimer |
by comparing molecular dynamics simulation of dimer and monomer, the indirect reasons for the inactivation of the monomer are found, that is the conformational variations of the active site in the monomer relative to dimer |
682785 |
3.4.22.69 | dimer |
dimerization is important for enzyme activity and only one active protomer in the dimer is enough for the catalysis |
680643 |
3.4.22.69 | dimer |
in solution the wild type protease exhibits both forms of monomer and dimer and the amount of the monomer is almost equal to that of the dimeric form |
692911 |
3.4.22.69 | dimer |
is only enzymatically active as a homodimer. Arg298 serves as a key component for maintaining dimerization, and consequently, its mutation will trigger a cooperative switch from a dimer to a monomer. The monomeric enzyme is irreversibly inactivated because its catalytic machinery is frozen in the collapsed state, characteristic of the formation of a short 310-helix from an active-site loop. Dimerization appears to be coupled to catalysis in 3CLpro through the use of overlapped residues for two networks, one for dimerization and another for the catalysis |
693918 |
3.4.22.69 | dimer |
one monomer per asymmetric unit, dimer is generated through the crystallographic twofold |
667075 |
3.4.22.69 | dimer |
SARS-CoV Mpro exists in solution as an equilibrium of both monomeric and dimeric forms, and the dimeric form is the enzymatically active form |
693917 |
3.4.22.69 | dimer |
the enzyme exists as a mixture of monomer and dimer at a higher protein concentration (4 mg/ml) and exclusively as a monomer at a lower protein concentration |
679408 |
3.4.22.69 | dimer |
the enzyme is only active in the dimeric form |
755284 |