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7  structures 124  species 1  interaction 167  sequences 2  architectures

Family: LEH (PF07858)

Summary: Limonene-1,2-epoxide hydrolase catalytic domain

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This is the Wikipedia entry entitled "Limonene-1,2-epoxide hydrolase". More...

Limonene-1,2-epoxide hydrolase Edit Wikipedia article

Limonene-1,2-epoxide hydrolase catalytic domain
PDB 1nww EBI.jpg
limonene-1,2-epoxide hydrolase
Identifiers
Symbol LEH
Pfam PF07858
Pfam clan CL0051
InterPro IPR013100
SCOP 1nww
SUPERFAMILY 1nww
OPM superfamily 141
OPM protein 2bng
limonene-1,2-epoxide hydrolase
Identifiers
EC number 3.3.2.8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a limonene-1,2-epoxide hydrolase (EC 3.3.2.8) is an enzyme that catalyzes the chemical reaction

limonene-1,2-epoxide + H2O \rightleftharpoons limonene-1,2-diol

Thus, the two substrates of this enzyme are limonene-1,2-epoxide and H2O, whereas its product is limonene-1,2-diol.

This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is limonene-1,2-epoxide hydrolase. This enzyme is also called limonene oxide hydrolase. This enzyme participates in limonene and pinene degradation.

Epoxide hydrolases catalyse the hydrolysis of epoxides to corresponding diols, which is important in detoxification, synthesis of signal molecules, or metabolism. Limonene-1,2- epoxide hydrolase (LEH) differs from many other epoxide hydrolases in its structure and its novel one-step catalytic mechanism. Its main fold consists of a six-stranded mixed beta-sheet, with three N-terminal alpha helices packed to one side to create a pocket that extends into the protein core. A fourth helix lies in such a way that it acts as a rim to this pocket. Although mainly lined by hydrophobic residues, this pocket features a cluster of polar groups that lie at its deepest point and constitute the enzymes active site.[1]

References[edit]

  1. ^ Arand M, Hallberg BM, Zou J, Bergfors T, Oesch F, van der Werf MJ, de Bont JA, Jones TA, Mowbray SL (June 2003). "Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site". EMBO J. 22 (11): 2583–92. doi:10.1093/emboj/cdg275. PMC 156771. PMID 12773375. 

Further reading[edit]

This article incorporates text from the public domain Pfam and InterPro IPR013100

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Limonene-1,2-epoxide hydrolase catalytic domain Provide feedback

Epoxide hydrolases catalyse the hydrolysis of epoxides to corresponding diols, which is important in detoxification, synthesis of signal molecules, or metabolism. Limonene-1,2- epoxide hydrolase (LEH) differs from many other epoxide hydrolases in its structure and its novel one-step catalytic mechanism. Its main fold consists of a six-stranded mixed beta-sheet, with three N-terminal alpha helices packed to one side to create a pocket that extends into the protein core. A fourth helix lies in such a way that it acts as a rim to this pocket. Although mainly lined by hydrophobic residues, this pocket features a cluster of polar groups that lie at its deepest point and constitute the enzyme's active site [1].

Literature references

  1. Arand M, Hallberg BM, Zou J, Bergfors T, Oesch F, van der Werf MJ, de Bont JA, Jones TA, Mowbray SL; , EMBO J 2003;22:2583-2592.: Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site. PUBMED:12773375 EPMC:12773375


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013100

Epoxide hydrolases catalyse the hydrolysis of epoxides to corresponding diols, which is important in detoxification, synthesis of signal molecules, or metabolism. Limonene-1,2- epoxide hydrolase (LEH) differs from many other epoxide hydrolases in its structure and its novel one-step catalytic mechanism. Its main fold consists of a six-stranded mixed beta-sheet, with three N-terminal alpha helices packed to one side to create a pocket that extends into the protein core. A fourth helix lies in such a way that it acts as a rim to this pocket. Although mainly lined by hydrophobic residues, this pocket features a cluster of polar groups that lie at its deepest point and constitute the enzymes active site [PUBMED:12773375].

Domain organisation

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Pfam Clan

This family is a member of clan NTF2 (CL0051), which has the following description:

This superfamily contains a variety of enzymes such as Scytalone dehydratase, Delta-5-3-ketosteroid isomerase, Limonene-1,2-epoxide hydrolase among others. The family also includes presumed non-enzymatic homologues such as NTF2.

The clan contains the following 24 members:

CaMKII_AD DUF1348 DUF2358 DUF3225 DUF3804 DUF4440 DUF4467 LEH Lumazine_bd Lumazine_bd_2 MBA1 MecA_N Mtr2 NTF2 PHZA_PHZB Ring_hydroxyl_B Scytalone_dh SnoaL SnoaL_2 SnoaL_3 SnoaL_4 Tim44 VirB8 WI12

Alignments

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(7)
Full
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Representative proteomes NCBI
(472)
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RP55
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  Seed
(7)
Full
(167)
Representative proteomes NCBI
(472)
Meta
(122)
RP15
(8)
RP35
(30)
RP55
(36)
RP75
(43)
Alignment:
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  Seed
(7)
Full
(167)
Representative proteomes NCBI
(472)
Meta
(122)
RP15
(8)
RP35
(30)
RP55
(36)
RP75
(43)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Pfam alignments:

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_15033 (release 14.0)
Previous IDs: none
Type: Domain
Author: Fenech M
Number in seed: 7
Number in full: 167
Average length of the domain: 120.10 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 83.09 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.6 21.6
Trusted cut-off 21.6 21.6
Noise cut-off 21.5 21.5
Model length: 125
Family (HMM) version: 7
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

LEH

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the LEH domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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