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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1qsg

E.C. nameenoyl-[acyl-carrier-protein] reductase (NADH)
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 1.3.1.9
CSA Homologues of 1qsgThere are 410 Homologs
CSA Entries With UniProtID P0AEK4
CSA Entries With EC Number 1.3.1.9
PDBe Entry 1qsg
PDBSum Entry 1qsg
MACiE Entry 1qsg

Literature Report

IntroductionEnoyl ACP reductase catalyses the last step in fatty acid biosynthesis where trans enoyl ACP is reduced to form acylACP. The bacterial form of the enzyme is different from the human form as it exists as a free globular protein rather than a part of a multienzyme complex. Therefore inhibitors of the bacterial form could be useful as antibiotics.
MechansimThe bacterial enzyme uses either NADH or NADPH as a cofactor for the reduction, whereby hydrogen transfer to the 3-Carbon of the double bond occurs resulting in an enolate intermediate, stabilised by hydrogen bonding to a Tyrosine and a nearby Lysine. Subsequent protonation of the oxygen by the tyrosine leads to the enol tautomer of the product.
Reaction

Catalytic Sites for 1qsg

Annotated By Reference To The Literature - Site 6 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrA156156macie:sideChainThe OH group of the tyrosine forms a hydrogen bond to the oxygen of the enolate intermediate, to allow hydride transfer from the cofactor to the substrate. The proton of the OH group is then donated to the substrate to form the enol form of the product.
LysA163163macie:sideChainThe positive form of the lysine residue acts to stabilise the enolate intermediate to allow hydride transfer from the cofactor to the substrate to take place.

Annotated By Reference To The Literature - Site 7 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrB156156macie:sideChainThe OH group of the tyrosine forms a hydrogen bond to the oxygen of the enolate intermediate, to allow hydride transfer from the cofactor to the substrate. The proton of the OH group is then donated to the substrate to form the enol form of the product.
LysB163163macie:sideChainThe positive form of the lysine residue acts to stabilise the enolate intermediate to allow hydride transfer from the cofactor to the substrate to take place.

Annotated By Reference To The Literature - Site 8 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrC156156macie:sideChainThe OH group of the tyrosine forms a hydrogen bond to the oxygen of the enolate intermediate, to allow hydride transfer from the cofactor to the substrate. The proton of the OH group is then donated to the substrate to form the enol form of the product.
LysC163163macie:sideChainThe positive form of the lysine residue acts to stabilise the enolate intermediate to allow hydride transfer from the cofactor to the substrate to take place.

Annotated By Reference To The Literature - Site 9 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrD156156macie:sideChainThe OH group of the tyrosine forms a hydrogen bond to the oxygen of the enolate intermediate, to allow hydride transfer from the cofactor to the substrate. The proton of the OH group is then donated to the substrate to form the enol form of the product.
LysD163163macie:sideChainThe positive form of the lysine residue acts to stabilise the enolate intermediate to allow hydride transfer from the cofactor to the substrate to take place.

Annotated By Reference To The Literature - Site 10 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrE156156macie:sideChainThe OH group of the tyrosine forms a hydrogen bond to the oxygen of the enolate intermediate, to allow hydride transfer from the cofactor to the substrate. The proton of the OH group is then donated to the substrate to form the enol form of the product.
LysE163163macie:sideChainThe positive form of the lysine residue acts to stabilise the enolate intermediate to allow hydride transfer from the cofactor to the substrate to take place.

Annotated By Reference To The Literature - Site 11 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrF156156macie:sideChainThe OH group of the tyrosine forms a hydrogen bond to the oxygen of the enolate intermediate, to allow hydride transfer from the cofactor to the substrate. The proton of the OH group is then donated to the substrate to form the enol form of the product.
LysF163163macie:sideChainThe positive form of the lysine residue acts to stabilise the enolate intermediate to allow hydride transfer from the cofactor to the substrate to take place.

Annotated By Reference To The Literature - Site 12 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrG156156macie:sideChainThe OH group of the tyrosine forms a hydrogen bond to the oxygen of the enolate intermediate, to allow hydride transfer from the cofactor to the substrate. The proton of the OH group is then donated to the substrate to form the enol form of the product.
LysG163163macie:sideChainThe positive form of the lysine residue acts to stabilise the enolate intermediate to allow hydride transfer from the cofactor to the substrate to take place.

Annotated By Reference To The Literature - Site 13 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrH156156macie:sideChainThe OH group of the tyrosine forms a hydrogen bond to the oxygen of the enolate intermediate, to allow hydride transfer from the cofactor to the substrate. The proton of the OH group is then donated to the substrate to form the enol form of the product.
LysH163163macie:sideChainThe positive form of the lysine residue acts to stabilise the enolate intermediate to allow hydride transfer from the cofactor to the substrate to take place.

Literature References

Notes:
Baldock C
The X-ray structure of Escherichia coli enoyl reductase with bound NAD+ at 2.1 A resolution.
J Mol Biol 1998 284 1529-1546
PubMed: 9878369
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