The succinyl-CoA substrate must already be in the active site. A free phosphate enters the active site and using one of it's oxygen atoms attacks the carbonyl of the thioester. this displaces the pair of electrons in the C-S bond which swing out to grah a proton from a nearby acid, A HIS in this case.
The results of the first reaction are shown. A phosphoanhydride has formed between succinate and the phosphate (phosphate on an organic acid) and the nearby HIS is in the base state.
The base form of the histidine now attacks the phopshoanhydride. displacing the succinate.
the results of the above reaction are shown. The HIS has a phosphate covalently attached - note a N-P bond here. the succinate is free to leave the active site of the enzyme
GDP enters the active site. (represented as GMP-PO4). The terminal phosphate attackes the phosphate of the phosphohistidine displacing the histidine.
The final results are shown. GTP has formed and histidine is back to its normal state.
Reaction | Rationale | Thermodynamics | Mechanism | Pictures | JMOL |
Enzyme Name |
Succinyl-CoA Synthetase |
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Reaction Catalyzed |
two step reaction:
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Reaction Type |
Two Step Reaction
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Pathway Involvement | Citric Acid Cycle
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Cofactors/Cosubstrates | The ADP "equivalent" GDP and PO4= (phosphate) are co-substrates and the ATP "equivalent" GTP and coenzyme A are co-products. no other cofactors are required |