NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria of the rat

Biochim Biophys Acta. 1989 Sep 11;1005(1):13-9. doi: 10.1016/0005-2760(89)90025-8.


Acyl-CoA hydrolase activity was studied in brown adipose tissue (BAT) mitochondria of rats. The substrate specificity was investigated: total hydrolase activity showed two activity peaks, one sharp peak for propionyl-CoA and a broad peak at medium- to long-chain acyl-CoAs. The propionyl-CoA activity fully comigrated with a mitochondrial matrix marker enzyme in fractionation studies of tissue and mitochondria. The hydrolytic activity against short-chain acyl-CoAs was inhibited by NADH, and analyses of the substrate specificity of the hydrolases in the presence and absence of NADH allowed for the delineation of two distinct acyl-CoA hydrolases. These hydrolases could also be separated by gel filtration. It was concluded that rat BAT mitochondria possess at least two matrix acyl-CoA hydrolases: one broad-spectrum acyl-CoA hydrolase with an apparent native molecular weight of less than 100,000, and a specific propionyl-CoA hydrolase with an apparent native molecular weight at least 240,000; this hydrolase is regulated by NADH. It is suggested that the function of the propionyl-CoA hydrolase is to ensure that the level of propionyl-CoA in the mitochondria is not detrimentally increased.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipose Tissue, Brown / enzymology*
  • Animals
  • Chromatography, Gel
  • Female
  • Kinetics
  • Mitochondria / enzymology*
  • NAD / pharmacology*
  • Oxidation-Reduction
  • Palmitoyl-CoA Hydrolase / isolation & purification
  • Palmitoyl-CoA Hydrolase / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Substrate Specificity
  • Thiolester Hydrolases / isolation & purification
  • Thiolester Hydrolases / metabolism*


  • NAD
  • Thiolester Hydrolases
  • propionyl CoA hydrolase
  • Palmitoyl-CoA Hydrolase