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- W1978889674 abstract "Most prokaryotic phosphofructokinases (PFKs), like those from Bacillus stearothermolphilus (BsPFK) and E.coli (EcPFK), exhibit both tight binding affinity for the allosteric inhibitor phosphoenolpyruvate (PEP) and strong inhibition. PFK from Lactobacillus delbrueckii subspecies bulgaricus (LbPFK), which is similar in structure and sequence to BsPFK and EcPFK, exhibits weak PEP binding, with the strength of the inhibition being indeterminate. D12, found along the active site interface, is conserved in over 150 prokaryotic PFKs, and it forms hydrogen bonds with highly conserved residues across this interface. Mutating D12 to alanine in BsPFK enhances PEP binding by 100-fold with no change in the extent of PEP inhibition. When D12A was introduced into LbPFK only a 5-fold enhancement in PEP binding was observed. Crystal structures of D12A BsPFK and D12A LbPFK were solved to 2.4 A resolution. Comparison of D12A and wild-type BsPFK with fructose 6-phosphate bound shows a quaternary shift along the active site interface, breaking the hydrogen bonds involving D12. By contrast, D12A LbPFK exhibits no major change in structure relative to wild type BsPFK. In hopes of further enhancing PEP binding, the following mutations of non-conserved residues in the allosteric site were made to the corresponding residues in either EcPFK or BsPFK, respectively. H59D, E55Y, D187E and S319Y combined showed no enhancement in PEP binding. S211R, D214K and G216S alone and in combination also had no effect on PEP binding. All these mutations suggest that the diminished PEP binding affinity to LbPFK is the consequence of more that just the residues in the allosteric site, likely involving the resistance of this enzyme to undergoing the quaternary shift. Funding came from NIH grant GM33216, NIH CBI training grant, and the Welch Foundation grant A1543." @default.
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- W1978889674 date "2009-02-01" @default.
- W1978889674 modified "2023-09-29" @default.
- W1978889674 title "Weak Binding of Phospho(enol)pyruvate to Phosphofructokinase from Lactobacillus delbrueckii" @default.
- W1978889674 doi "https://doi.org/10.1016/j.bpj.2008.12.2278" @default.
- W1978889674 hasPublicationYear "2009" @default.
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