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Discussion Starter · #1 ·
The rule is that a "kinase" enzyme uses ATP to transfer one of its phosphate groups to a substrate.
E.g. Glucokinase, Phosphofructokinase etc.
Then how come "Pyruvate Kinase" doesn't do so. Instead the reaction it catalyzes (PEP -----> Pyruvate) actually yields ATP instead of utilizing it?
Can someone please explain the concept behind this.
Thanks a lot
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