Physiochemical properties of the long-chain-acyl-CoA hydrolase from rat liver microsomes.
The physicochemical properties of a long-chain-acyl-CoA hydrolase (EC 3.1.2.2) of rat liver microsomes have been studied. The hydrolase sedimented as a homogeneous species with a sedimentation coefficient, S20,W, of 4.1 S and the molecular weight of 59000 was obtained. Amino acid composition of the enzyme was determined. The specific absorption coefficient, A280nm1% was estimated as 9.8 (1 cm cell length) and the circular dichroic data suggested 50-60% alpha-helical structure. The enzyme contained three sulphydryl groups, and one of these was exposed to the environment. The hydrolase was inhibited by the serine-directed reagent phenylmethylsulfonyl fluoride, as well as p-hydroxymercuribenzoate, N-ethylmaleimide and 5,5'-dithiobis(2-nitrobenzoic acid). Reactivation by means of dithiothreitol was never complete with phenylmethylsulfonyl fluoride and p-hydroxymercuribenzoate as inhibitors.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002413:Cations, Divalent; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology*; D008970:Molecular Weight; D010170:Palmitoyl-CoA Hydrolase / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D012694:Serine; D013869:Thiolester Hydrolases / Q000378:metabolism*
D000596:Amino Acids; D002413:Cations, Divalent; D012694:Serine; D013869:Thiolester Hydrolases; D010170:Palmitoyl-CoA Hydrolase