the recombinant and wild type enzyme exhibit heterogeneity of the quaternary structure and in solution exist in three interconvertible forms, namely, monomeric, homodimeric, and homotetrameric. The monomer/dimer/tetramer ratios depended on protein concentration and fall within the range from 72:27:1 to 39:23:38. The enzyme is fully active in each of the oligomeric structures
6 * 29700, enzyme is a trimer of disulphide-linked dimers, three interchain disulfide bonds in the enzyme molecule are formed between Cys residues at position 219, SDS-PAGE
Staphylococcus aureus NagB is active without the need for allosteric activation. No rate increase is observed when N-acetylglucosamine-6-phosphate (the allosteric activator for Escherichia coli NagB) is added to the assay mixture, or when incubated with the enzyme prior to adding it to the assay
Staphylococcus aureus NagB is active without the need for allosteric activation. No rate increase is observed when N-acetylglucosamine-6-phosphate (the allosteric activator for Escherichia coli NagB) is added to the assay mixture, or when incubated with the enzyme prior to adding it to the assay
Staphylococcus aureus NagB is active without the need for allosteric activation. No rate increase is observed when N-acetylglucosamine-6-phosphate (the allosteric activator for Escherichia coli NagB) is added to the assay mixture, or when incubated with the enzyme prior to adding it to the assay