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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1pfk

E.C. name6-phosphofructokinase
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 2.7.1.11
CSA Homologues of 1pfkThere are 11 Homologs
CSA Entries With UniProtID P0A796
CSA Entries With EC Number 2.7.1.11
PDBe Entry 1pfk
PDBSum Entry 1pfk
MACiE Entry 1pfk

Literature Report

Introduction Phosphofructokinase (PFK) is a key enzyme in glycolysis. It transfers a phosphate group to fructose and in doing so controls entry into the pathway. PFK is highly regulated and is cooperative for fructose and shows allosteric inhibition by phosphoenolpyruvate and activation by ADP. The enzyme changes from the R state to the T state by a rotation around the 'p' axis of the molecule, resulting in a change in the subunit-subunit interactions that are communicated to the active site.
The ATP binding site remains fixed during the transition from R to T state except for the residue arg 72 that is important for bridging the substrate phosphates during catalysis. In the T state this Arg residue forms a salt bridge with glu241. The T state is also characterised by a large change in the substrate binding site, the movement of the '6-F' loop leads to the collapse of this binding site.
MechansimNo mechanism proposed
Reaction

Catalytic Sites for 1pfk

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GlyA1112macie:mainChainAmide
AspA127128macie:sideChain
ThrA125126macie:sideChain
ArgA7273macie:sideChain
ArgA171172macie:sideChain

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GlyB1112macie:mainChainAmide
AspB127128macie:sideChain
ThrB125126macie:sideChain
ArgB7273macie:sideChain
ArgB171172macie:sideChain

Literature References

Notes:
Rypniewski WR.
Crystal structure of unliganded phosphofructokinase from Escherichia coli
J Mol Biol 1989 207 805-821
PubMed: 2527305
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