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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1dci

E.C. namedelta(3,5)-delta(2,4)-dienoyl-CoA isomerase
SpeciesRattus norvegicus (Rat)
E.C. Number (IntEnz) 5.3.3.-
CSA Homologues of 1dciThere are 47 Homologs
CSA Entries With UniProtID Q62651
CSA Entries With EC Number 5.3.3.-
PDBe Entry 1dci
PDBSum Entry 1dci
MACiE Entry M0342

Literature Report

IntroductionFatty acids are metabolised by sequential removal of two-carbon units by oxidation at the beta-carbon. Only saturated fatty acids or unsaturated fatty acids with double bonds extending from even-numbered carbon atoms can enter the main beta-oxidation pathway, so double bonds at odd-numbered carbon atoms in unsaturated fatty acids has to be converted to even-numbered double bonds to enter beta-oxidation. Dienoyl-CoA isomerase catalyses the conversion of 3-trans,5-cis dienoyl-CoA into 2-trans,4-trans dienoyl-CoA.
MechansimGlu196 acts as a base to abstract a proton from C2 to initiate the shifting of the double bonds. Asp204 donates a proton to C6 to complete the reaction.

Catalytic Sites for 1dci

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA204204macie:sideChainIt acts as an acid to donate a proton to C6.
GluA196196macie:sideChainIt acts as a base to abstract a proton from C2.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspB204204macie:sideChainIt acts as an acid to donate a proton to C6.
GluB196196macie:sideChainIt acts as a base to abstract a proton from C2.

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspC204204macie:sideChainIt acts as an acid to donate a proton to C6.
GluC196196macie:sideChainIt acts as a base to abstract a proton from C2.

Literature References

Notes:
Modis Y
The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis.
Structure 1998 6 957-970
PubMed: 9739087
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