Group Transfer Reaction - Both ADP and 1,3 bisphosphoglycerate must bind to the active site
The terminal phosphate of ADP attacks the phosphate on the organic acid of glycerate. and a pair of electrons leaves the P-O bond and ends up on the "O" of the organic acid
The results of the previous steps are shown. The phosphate has moved to ATP and 3-phosphoglycerate is also left behind.

| Reaction | Rationale | Thermodynamics | Mechanism | Pictures | JMOL |
|
Enzyme Name |
Glycerate Kinase |
|
|
|
||
|
Reaction Catalyzed |
Group Transfer from 1,3 bisphosphoglycerate to ADP to make ATP
|
|
|
Reaction Type |
Group Transfer |
|
|
Pathway Involvement |
Glycolysis AND gluconeogenesis |
|
|
Cofactors/Cosubstrates |
ADP is a cosubstrate in glycolysis direction and ATP is a coproduct |
|