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In enzymology, 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) is an enzyme that catalyzes the chemical reaction

β-hydroxybutyryl-CoA
R=CH3
+ NADP+
 
 
 
H+
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
H+
 
acetoacetyl-CoA
R=CH3
+ NADPH
 


The two substrates of this enzyme are β-hydroxybutyryl-CoA and oxidised nicotinamide adenine dinucleotide phosphate (NADP+). Its products are acetoacetyl-CoA, reduced NADPH, and a proton.[1][2]

This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase. Other names in common use include beta-hydroxybutyryl coenzyme A dehydrogenase, L-(+)-3-hydroxybutyryl-CoA dehydrogenase, BHBD, dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine, dinucleotide phosphate), L-(+)-3-hydroxybutyryl-CoA dehydrogenase, and beta-hydroxybutyryl-CoA dehydrogenase. This enzyme participates in benzoate degradation via coa ligation and butanoate metabolism.

References

  1. ^ Enzyme 1.1.1.157 at KEGG Pathway Database.
  2. ^ Madan VK, Hillmer P, Gottschalk G (1973). “Purification and properties of NADP-dependent L(+)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri“. Eur. J. Biochem. 32 (1): 51–6. doi:10.1111/j.1432-1033.1973.tb02577.x. PMID 4405720.