Multiple forms of carboxylesterase activity in Acinetobacter calcoaceticus.
A carboxylesterase activity (E.C.3.1.1) was found in all four strains of Acinetobacter calcoaceticus tested. The activity was present in both 2 X 10(4) gav h-1 supernatant and bacterial wall-membrane fractions. The activity in the supernatant was in two molecular weight forms, the predominant form with a Mr of about 10(3) K and a minor form Mr approximately 600 K. The activity was inhibited by phenylmethylsulfonyl fluoride. SDS-PAGE showed that in A. calcoaceticus NCIB 8250 the activity was composed of three components of Mr 43, 40 and 38 K. The individual components showed different activities with 1- or 2-naphthyl esters. Of the other strains used, one showed a nearly identical pattern of component activities, while the other two showed only two component activities.
Sherwani
M K
MK
Department of Biochemistry, University of Glasgow, Scotland, U.K.
Fixter
L M
LM
D000150:Acinetobacter / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000032:analysis*; D008970:Molecular Weight
D002265:Carboxylic Ester Hydrolases