Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.127
Description:Linalool dehydratase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.127
BRENDA Enzyme Link: BRENDA 4.2.1.127
KEGG Enzyme Link: KEGG4.2.1.127
BioCyc Enzyme Link: BioCyc 4.2.1.127
ExPASy Enzyme Link: ExPASy4.2.1.127
EC2PDB Enzyme Link: EC2PDB 4.2.1.127
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.127
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.127
IntEnz Enzyme Link: IntEnz 4.2.1.127
MEDLINE Enzyme Link: MEDLINE 4.2.1.127
MSA:

4.2.1.127;

Phylogenetic Tree:

4.2.1.127;

Uniprot:
M-CSA:
RHEA:30711 (S)-linalool = beta-myrcene + H2O
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[CH3;+0:4])-[OH;+0:5]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH2;+0:4].[OH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Microbial monoterpene transformations-a review.Marmulla R, Harder J201425076942
Enantiospecific (S)-(+)-linalool formation from beta-myrcene by linalool dehydratase-isomerase.Lüddeke F, Harder J2011 Jul-Aug21950166
Linalool dehydratase-isomerase, a bifunctional enzyme in the anaerobic degradation of monoterpenes.Brodkorb D, Gottschall M, Marmulla R, Lüddeke F, Harder J2010 Oct 120663876