EC number:4.2.1.134

Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.134
Description:Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase.
Cath: 3.10.20.90;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.134
BRENDA Enzyme Link: BRENDA 4.2.1.134
KEGG Enzyme Link: KEGG4.2.1.134
BioCyc Enzyme Link: BioCyc 4.2.1.134
ExPASy Enzyme Link: ExPASy4.2.1.134
EC2PDB Enzyme Link: EC2PDB 4.2.1.134
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.134
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.134
IntEnz Enzyme Link: IntEnz 4.2.1.134
MEDLINE Enzyme Link: MEDLINE 4.2.1.134

EC number:4.2.1.134

MSA:

4.2.1.134;
Phylogenetic Tree:

4.2.1.134;
Uniprot:
M-CSA:
RHEA:45812 a very-long-chain (3R)-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[OH;+0:3])-[CH2;+0:4]-[*:5]>>[*:1]-[CH;+0:2]=[CH;+0:4]-[*:5].[OH2;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The very-long-chain hydroxy fatty acyl-CoA dehydratase PASTICCINO2 is essential and limiting for plant development.Bach L, Michaelson LV, Haslam R, Bellec Y, Gissot L, Marion J, Da Costa M, Boutin JP, Miquel M, Tellier F, Domergue F, Markham JE, Beaudoin F, Napier JA, Faure JD2008 Sep 2318799749
Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation.Kihara A, Sakuraba H, Ikeda M, Denpoh A, Igarashi Y2008 Apr 2518272525