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. Author manuscript; available in PMC: 2019 Jun 1.
Published in final edited form as: Nat Chem Biol. 2018 Oct 29;14(12):1127–1132. doi: 10.1038/s41589-018-0153-x

Figure 4. Proposed catalytic cycle of PCS.

Figure 4

In the open conformation, 3-hydroxypropionate (3OHP) and ATP are converted to 3-hydroxypropionyl-AMP (3OHP-AMP) through the ligase domain (orange). The binding of CoA induces closing of the enzyme and the formation of 3-hydroxypropionyl-CoA (3OHP-CoA). 3OHP-CoA is released into the reaction chamber, where it is converted by the dehydratase domain (purple) to acrylyl-CoA. Acrylyl-CoA then enters the active site of the reductase domain (cyan). Following the reduction of acrylyl-CoA to propionyl-CoA, the reaction chamber reopens to release propionyl-CoA, which leaves PCS ready for the next catalytic cycle.