Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.120
Description:4-hydroxybutanoyl-CoA dehydratase.
Cath: 1.10.3140.10; 1.20.140.10; 2.40.110.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.120
BRENDA Enzyme Link: BRENDA 4.2.1.120
KEGG Enzyme Link: KEGG4.2.1.120
BioCyc Enzyme Link: BioCyc 4.2.1.120
ExPASy Enzyme Link: ExPASy4.2.1.120
EC2PDB Enzyme Link: EC2PDB 4.2.1.120
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.120
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.120
IntEnz Enzyme Link: IntEnz 4.2.1.120
MEDLINE Enzyme Link: MEDLINE 4.2.1.120
MSA:

4.2.1.120;

Phylogenetic Tree:

4.2.1.120;

Uniprot:
M-CSA:
RHEA:26530 4-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH2;+0:3]-[CH2;+0:4]-[OH;+0:5]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[CH3;+0:4].[OH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis involving a [4Fe-4S] cluster and flavin.Martins BM, Dobbek H, Cinkaya I, Buckel W, Messerschmidt A2004 Nov 215496473
4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: characterization of FAD and iron-sulfur clusters involved in an overall non-redox reaction.Müh U, Cinkaya I, Albracht SP, Buckel W1996 Sep 108794752
Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA delta 3-delta 2-isomerase from Clostridium aminobutyricum.Scherf U, Buckel W1993 Jul 158344309
Assay of 4-hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum.Willadsen P, Buckel W1990 Jul2227355
A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea.Berg IA, Kockelkorn D, Buckel W, Fuchs G2007 Dec 1418079405