4-hydroxybutanoyl-CoA dehydratase

4-hydroxybutanoyl-CoA dehydratase (EC 4.2.1.120) is an enzyme with systematic name 4-hydroxybutanoyl-CoA hydro-lyase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

4-hydroxybutanoyl-CoA (E)-but-3-enoyl-CoA + H2O
4-hydroxybutanoyl-CoA dehydratase
Identifiers
EC no.4.2.1.120
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

This enzyme contains FAD and a [4Fe-4S] iron-sulfur cluster.

References
  1. Bartsch RG, Barker HA (January 1961). "A vinylacetyl isomerase from Clostridium kluyveri". Archives of Biochemistry and Biophysics. 92: 122–32. doi:10.1016/0003-9861(61)90226-0. PMID 13687513.
  2. Scherf U, Söhling B, Gottschalk G, Linder D, Buckel W (1994). "Succinate-ethanol fermentation in Clostridium kluyveri: purification and characterisation of 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA delta 3-delta 2-isomerase". Archives of Microbiology. 161 (3): 239–45. doi:10.1007/bf00248699. PMID 8161284.
  3. Scherf U, Buckel W (July 1993). "Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA delta 3-delta 2-isomerase from Clostridium aminobutyricum". European Journal of Biochemistry. 215 (2): 421–9. doi:10.1111/j.1432-1033.1993.tb18049.x. PMID 8344309.
  4. Müh U, Cinkaya I, Albracht SP, Buckel W (September 1996). "4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: characterization of FAD and iron-sulfur clusters involved in an overall non-redox reaction". Biochemistry. 35 (36): 11710–8. doi:10.1021/bi9601363. PMID 8794752.
  5. Berg IA, Kockelkorn D, Buckel W, Fuchs G (December 2007). "A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea". Science. 318 (5857): 1782–6. doi:10.1126/science.1149976. PMID 18079405.
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