_EC 4.2.1.120 4-hydroxybutanoyl-CoA dehydratase. 1 PDB entries  
EC 4.-.-.- Lyases. [3,640 PDB entries]
EC 4.2.-.- Carbon-oxygen lyases. [1,777 PDB entries]
EC 4.2.1.- Hydro-lyases. [1,381 PDB entries]
EC 4.2.1.120 4-hydroxybutanoyl-CoA dehydratase. [1 PDB entries]    
1u8v

Reaction: 4-hydroxybutanoyl-CoA = but-3-enoyl-CoA + H(2)O.
 


4-hydroxybutanoyl-CoA
=
but-3-enoyl-CoA
+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Cofactor(s): FAD; Iron-sulfur.
 

FAD

Iron-sulfur
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: The enzyme is often present as a bifunctional enzyme, catalyzing the dehydration of 4-hydroxybutanoyl-CoA to but-3-enoyl-CoA followed by isomerization of the later to crotonyl-CoA (EC 5.3.3.3). The enzyme has been characterized from several microorganisms, including Clostridium kluyveri, where it participates in succinate fermentation, Clostridium aminobutyricum, where it participates in 4-aminobutyrate degradation, and Metallosphaera sedula, where it participates in the 3-hydroxypropanoate/4-hydroxybutyrate cycle, an autotrophic CO(2) fixation pathway found in some thermoacidophilic archaea.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 1 PDB entries in enzyme class E.C.4.2.1.120

  PDB code Protein
1u8v
Crystal structure of 4-hydroxybutyryl-coa dehydratase from clostridium aminobutyricum: radical catalysis involving a [4fe-4s] cluster and flavin
Source: Clostridium aminobutyricum. Organism_taxid: 33953
Chains: A, B, C, D (490 residues) CATH domains: 1.10.3140.10 2.40.110.10 1.20.140.10
Bound ligand:   Het Group FAD is 45.00% similar to enzyme reactant but-3-enoyl-CoA