    3.5.99.6 | side-chain modification |
enzyme is chemically transaminated, modifying its N-terminal methionine residue to a 2-oxo-4-(methylthio)butyryl group, the transamination markedly reduces the affinity of the enzyme for its allosteric activator N-acetylglucosamine 6-phosphate, in contrast with the unmodified enzyme, which behaves as a typical allosteric K-enzyme, the modified enzyme becomes a mixed K-V allosteric protein, borohydride reduction to obtain the corresponding enzyme with a terminal hydroxy group, this enzyme shows significant recovery of the catalytic catalytic activity and its allosteric activation pattern, becomes similar to that found for the unmodified enzyme |
648238 |
