Biology:4-hydroxybutanoyl-CoA dehydratase

From HandWiki
Short description: Class of enzymes
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

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 [math]\displaystyle{ \rightleftharpoons }[/math] (E)-but-3-enoyl-CoA + H2O

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

References

  1. "A vinylacetyl isomerase from Clostridium kluyveri". Archives of Biochemistry and Biophysics 92: 122–32. January 1961. doi:10.1016/0003-9861(61)90226-0. PMID 13687513. 
  2. "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. 1994. doi:10.1007/bf00248699. PMID 8161284. 
  3. "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. July 1993. doi:10.1111/j.1432-1033.1993.tb18049.x. PMID 8344309. 
  4. "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. September 1996. doi:10.1021/bi9601363. PMID 8794752. http://dare.uva.nl/personal/pure/en/publications/4hydroxybutyrylcoa-dehydratase-from-clostridium-aminobytyricum-characterization-of-fad-and-iron-sulfur-clusters-involved-in-an-overall-nonredox-reaction(506b07fa-616f-4cba-9001-8016c7f99218).html. 
  5. "A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea". Science 318 (5857): 1782–6. December 2007. doi:10.1126/science.1149976. PMID 18079405. 

External links