4-hydroxybutanoyl-CoA dehydratase

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4-hydroxybutanoyl-CoA dehydratase
Identifiers
EC number 4.2.1.120
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB 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 but-3-enoyl-CoA + H2O

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

References[edit]

  1. ^ Bartsch, R.G.; Barker, H.A. (1961). "A vinylacetyl isomerase from Clostridium kluyveri". Arch. Biochem. Biophys. 92: 122–132. PMID 13687513. doi:10.1016/0003-9861(61)90226-0. 
  2. ^ Scherf, U.; Sohling, B.; Gottschalk, G.; Linder, D.; Buckel, W. (1994). "Succinate-ethanol fermentation in Clostridium kluyveri: purification and characterisation of 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ32-isomerase". Arch. Microbiol. 161 (3): 239–245. PMID 8161284. doi:10.1007/bf00248699. 
  3. ^ Scherf, U.; Buckel, W. (1993). "Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ32-isomerase from Clostridium aminobutyricum". Eur. J. Biochem. 215 (2): 421–429. PMID 8344309. doi:10.1111/j.1432-1033.1993.tb18049.x. 
  4. ^ Muh, U.; Cinkaya, I.; Albracht, S.P.; Buckel, W. (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): 11710–11718. PMID 8794752. doi:10.1021/bi9601363. 
  5. ^ Berg, I.A.; Kockelkorn, D.; Buckel, W.; Fuchs, G. (2007). "A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea". Science. 318: 1782–1786. PMID 18079405. doi:10.1126/science.1149976. 

External links[edit]