AlmA involved in the long-chain n -alkane degradation pathway in Acinetobacter baylyi ADP1 is a Baeyer-Villiger monooxygenase.

Many microbial studies on n -alkane degradation are focused on the genes involved in short-chain n -alkane (≤C16) degradation; however, reports on the genes involved in long-chain (LC) n -alkane (>C20) degradation are limited. Thus far, only AlmA has been reported to be involved in LC n -alkane degradation by Acinetobacter spp.; however, its role in the n -alkane degradation pathway remains elusive. In this study, we conducted a detailed characterization of AlmA in A. baylyi ADP1 and found that AlmA exhibits Baeyer-Villiger monooxygenase activity, thus indicating the presence of a novel LC n -alkane biodegradation mechanism in strain ADP1.