Abstract
ATP-dependent type 1 prokaryotic phosphofructokinase (PFK) catalyzes the conversion of fructose-6-phosphate (F6P) and MgATP to fructose-1,6-bisphosphate and MgADP. This enzyme is allosterically inhibited by phosphoenolpyruvate (PEP) and exists as a homotetramer with the four active sites formed along one dimer-dimer interface and four allosteric sites formed along the other. The overall structures of PFK's from E. coli, Bacillus stearothermophilus, and Lactobacillus delbruekii are very similar, and the sequences have high percent identity and similarity with Thermus thermophilus PFK.
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