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CSA entry for 1nu3
Original Entry
Title:
Hydrolase
Compound:
Limonene-1,2-epoxide hydrolase
Mutant:
Yes
UniProt/Swiss-Prot:
Q9ZAG3-LIMA_RHOER
EC Class:
3.3.2.8
Other CSA Entries:
Overview of all sites for 1nu3
Homologues of 1nu3
Entries for UniProt/Swiss-Prot: Q9ZAG3
Entries for EC: 3.3.2.8
Other Databases:
PDB entry: 1nu3
PDBsum entry: 1nu3
UniProt/Swiss-Prot: Q9ZAG3
IntEnz entry: 3.3.2.8
Literature Report:
Introduction:
Limonene-1,2-epoxide hydrolase(LEH) catalyses the hydrolysis of limonene-1,2-epoxide to limonene-1,2-diol. This enzyme allows the bacterium Rhodococcus erythropolis to grow on limonene as a sole source of carbon and energy. The hydrolysis catalysed by LEH is enantioconvergent, therefore attracting wide interest in industrial applications.
Mechanism:
The catalysis follows a single-step push-pull mechanism. The active site consists of a Asp-Arg-Asp triad. Asp132 acts as a base to deprotonate a water molecule, which performs a nucleophilic attack at one of the ring carbons, forcing epoxide ring opening. At the same time, Asp101 donates a proton to the oxygen atom of the epoxide ring to encourage the ring opening. Each carboxylate group of Asp132 and Asp101 maintains a pair of hydrogen bonds with guanidino group of Arg99 during the reaction and Arg99 acts as a proton shuttle to reverse the charge of Asp132 and Asp101 after the reaction.
Sites:

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Found by:
Literature reference 
PsiBLAST alignment on 1nww

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ARGA 99 99Sidechain
Acid/baseResidue
It acts as a proton shuttle to reverse the charge of Asp 132 and Asp 101 after the reaction.
Evidence from paper Evidence concerns Evidence type
PubMed ID 12773375 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 12773375 Current protein Mutagenesis of residue

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ASPA 101 101Sidechain
Acid/baseSubstrate
It acts as a base to protonate the oxygen atom of the epoxide to encourage ring opening.
Evidence from paper Evidence concerns Evidence type
PubMed ID 12773375 Current protein Residue is positioned appropriately (ligand position hypothetical)
PubMed ID 12773375 Current protein Mutagenesis of residue

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ASPA 132 132Sidechain
Acid/baseWater
It acts as a base to deprotonate a water molecule to promote its nucleophilic attack on one of the ring carbons, forcing epoxide ring opening.
Evidence from paper Evidence concerns Evidence type
PubMed ID 12773375 Current protein Mutagenesis of residue
PubMed ID 12773375 Current protein Residue is positioned appropriately (ligand position hypothetical)
References:
1
Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site.
M. Arand and B. M. Hallberg and J. Zou and T. Bergfors and F. Oesch and M. J. van der Werf and J. A. de Bont and T. A. Jones and S. L. Mowbray
EMBO J 22, (11) 2583-92, (2003).
12773375
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