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Catalytic Site Atlas

CSA LITERATURE entry for 1kzh

E.C. namediphosphate---fructose-6-phosphate 1-phosphotransferase
SpeciesBorrelia burgdorferi (Lyme disease spirochete)
E.C. Number (IntEnz) 2.7.1.90
CSA Homologues of 1kzh2f48,2hig,3f5m,3hno,3k2q,
CSA Entries With UniProtID
CSA Entries With EC Number 2.7.1.90
PDBe Entry 1kzh
PDBSum Entry 1kzh
MACiE Entry 1kzh

Literature Report

IntroductionThe Lyme disease causing Spirochete Borrelia burgdorferi uses pyrophosphate (PPi) rather than ATP as the source of phosphate for the phosphorylation of Fructose-6-phosphate to Fructose-1,6-bisphosphate in glycolysis. This strategy, common to many anaerobic bacteria, allows ATP to be conserved for other processes such as maintaining a proton gradient. The enzyme catalysing this process shares around 23% sequence identity to the E.coli PFK and many structural features differ between the two enzymes. However, the active sites do share a similar structure with conservation of key residues, so the mechanism of the reaction is almost certainly the same for each.
MechansimFructose-6-phosphate's 1COH acts as the nucleophile to attack the terminal phosphate of PPi. Its nucleophilicity is increased by the action of ASp 206 which removes a hydrogen ion from the attacking hydroxyl, allowing a pentavalent phosphate transition state to form, stabilised by Mg2+ and several conserved residues at the active site (Gly 82, Arg 146, Thr 204 and Lys 203). Collapse of the transition state results in the overall phosphoryl transfer occurring from PPi to fructose-6-phosphate
Reaction

Catalytic Sites for 1kzh

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ThrA204204macie:sideChainForms hydrogen bond to the PPi, thus can act to stabilise the negative charge that develops in formation of the pentavalent phosphate transition state.
AspA206206macie:sideChainActivates the 1-OH group of fructose-6-phosphate to allow the nucleophilic attack on the terminal phosphate of PPi which leads to the in-line phosphoryl transfer.
GlyA8282macie:mainChainAmideThe amide on the polypeptide backbone forms a strong hydrogen bond to the pyrophosphate thus stabilising the pentavalent phosphate transition state.
LysA203203macie:sideChainStabilises the pentavalent phosphate transition state through electrostatic interactions.
ArgA146146macie:sideChainContacts PPi through its positively charged side chain, thus stabilises the pentavalent phosphate transition state.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ThrB204204macie:sideChainForms hydrogen bond to the PPi, thus can act to stabilise the negative charge that develops in formation of the pentavalent phosphate transition state.
AspB206206macie:sideChainActivates the 1-OH group of fructose-6-phosphate to allow the nucleophilic attack on the terminal phosphate of PPi which leads to the in-line phosphoryl transfer.
GlyB8282macie:mainChainAmideThe amide on the polypeptide backbone forms a strong hydrogen bond to the pyrophosphate thus stabilising the pentavalent phosphate transition state.
LysB203203macie:sideChainStabilises the pentavalent phosphate transition state through electrostatic interactions.
ArgB146146macie:sideChainContacts PPi through its positively charged side chain, thus stabilises the pentavalent phosphate transition state.

Literature References

Notes:Magnesium ion is catalytic but was not present in the crystal structure.
Moore SA
The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi.
Structure 2002 10 659-671
PubMed: 12015149
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