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 but-3-enoyl-CoA + H2O
4-hydroxybutanoyl-CoA dehydratase
Identifiers
EC number4.2.1.120
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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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