H. Sztajer et al., BACTERIAL SHORT-CHAIN ACYL-COA OXIDASE - PRODUCTION, PURIFICATION ANDCHARACTERIZATION, Applied microbiology and biotechnology, 39(6), 1993, pp. 708-713
An Arthrobacter nicotianae strain has been found to produce an inducib
le acyl coenzyme A (CoA) oxidase. Nine times more butyryl-CoA oxidase
activity, compared to palmitoyl-CoA oxidase, was found in the cell ext
ract. The addition of flavin adenine dinucleotide (FAD) caused an incr
ease in acyl-CoA oxidase activity and thermal stability. The purified
enzyme exhibited a relative molecular mass of 50000 on sodium dodecyl
sulphate-polyacrylamide gel electrophoresis and 100000 under non-denat
uring conditions. Acyl-CoA oxidase from Arthrobacter nicotianae is hig
hly specific towards short-chain fatty acids. The fastest O2 uptake wa
s observed with butyryl-CoA as substrate. The enzyme is inhibited by s
ilver and mercury salts.