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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1bjp

E.C. name4-oxalocrotonate tautomerase
SpeciesPseudomonas putida (Bacteria)
E.C. Number (IntEnz) 5.3.2.-
CSA Homologues of 1bjpThere are 16 Homologs
CSA Entries With UniProtID Q01468
CSA Entries With EC Number 5.3.2.-
PDBe Entry 1bjp
PDBSum Entry 1bjp
MACiE Entry M0061

Literature Report

IntroductionThis entry covers 4-oxalocrotonate tautomerase (4-OT) and 5-Carboxymethyl-2-hydroxymuconate isomerase (CHMI), which catalyse the isomerisation of unsaturated ketones. The mechanism is common to both enzymes, although the substrates are different. There is no apparent sequence homology between them, although the active site pocket has conserved residues.
4-OT has only 62 residues in each chain, making it the smallest enzyme subunit known. The rate of catalysis approaches the diffusion-controlled limit. The gene for the enzyme is carried by the TOL plasmid in Pseudomonas putrida, and is involved in the catabolism of aromatic carbon sources.
MechansimThe N-terminal proline, is thought to act as a catalytic base (the only known enzyme for which this is the case). Arg40 and Arg12 are thought to stabilise the binding of the carboxylate groups on the substrate and Arg40 may also play a role in altering the pKa of Pro2.

Catalytic Sites for 1bjp

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ProA12macie:mainChainAmide
PheA5051macie:sideChain
ArgB3940macie:sideChain

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgA3940macie:sideChainError

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgC3940macie:sideChainError

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgD3940macie:sideChainError

Annotated By Reference To The Literature - Site 5 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgE3940macie:sideChainError

Annotated By Reference To The Literature - Site 6 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ProA12macie:mainChainAmide
PheA5051macie:sideChain
ArgB3940macie:sideChain

Annotated By Reference To The Literature - Site 7 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ProB12macie:sideChainError
PheB5051macie:sideChainError

Annotated By Reference To The Literature - Site 8 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ProC12macie:sideChainError
PheC5051macie:sideChainError

Annotated By Reference To The Literature - Site 9 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ProD12macie:sideChainError
PheD5051macie:sideChainError

Annotated By Reference To The Literature - Site 10 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ProE12macie:sideChainError
PheE5051macie:sideChainError

Literature References

Notes:
Subramanya HS
Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases.
Biochemistry 1996 35 792-802
PubMed: 8547259
Taylor AB
Crystal structure of 4-oxalocrotonate tautomerase inactivated by 2-oxo-3-pentynoate at 2.4 A resolution: analysis and implications for the mechanism of inactivation and catalysis.
Biochemistry 1998 37 14692-14700
PubMed: 9778344
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