EC Number |
Activating Compound |
Reference |
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1.13.11.8 | more |
allosteric rate enhancement in the presence of non-substrate protocatechuate-like aldehydes such as vanillin |
741768 |
1.13.11.8 | Vanillin |
heteroallosteric activation of LigAB by vanillin at an allosteric binding site in LigAB, regulatory feed-forward activation mechanism, kinetics, overview. Vanillin is the pre-pre-substrate of LigAB. Enhancement by vanillin is specific to protocatechuate. Glu86b is directly involved in a hydrogen bond network through the carboxylate with Ndelta of His127b, believed to be the catalytic base that performs the initial substrate deprotonation. The His127b methylene also contributes a small fraction to the identified allosteric binding pocket |
741768 |
1.13.11.8 | more |
impact of alpha-subunit Phe103alpha mutations on allosteric activation of alternate substrate dioxygenation by vanillin compared to the wild-type enzyme, overview |
743708 |
1.13.11.8 | Vanillin |
like the wild-type enzyme, F103T and F103V alpha-subunit point mutants also exhibit allosteric activation for the dioxygenation of protocatechuate and gallate, respectively |
743708 |