Entry M0190 188.8.131.52 isopentenyl-diphosphate delta-isomerase
The double bond of the isopentenyl diphosphate substrate deprotonates Tyr104.
Comment: The origin of the protonating H has not been conclusively stabilised. Glu116 is probably un-protonated given its location in the inner coordination sphere of the metal, there are also no order molecules observed that could serve as proton donors during this step. Thus it seems likely that the phenolic hydroxyl group in Tyr104 might be the source of the proton transferred to the double bond via Glu116 .
Amino acids involved in the reaction step.
Metal Cofactors involved in Step 01
||Bonds Changed in Order
||Atom Types Involved
The C-C bond changes from a double to single bond
View similar reactions in MACiE.