ABSTRACT
The aldehyde oxidase genes (aods) from Methylobacillus sp. KY4400 were cloned, and sequenced. The sequences for small (aodS, 489 bp), medium (aodM, 993 bp), and large (aodL, 2,328 bp) subunit genes were determined. At least one additional ORF was indispensable for the expression of enzyme activity. The structural genes contained two [2Fe-2S] centers, an FAD binding site, and a molybdenum cofactor binding site.
Subject(s)
Aldehyde Oxidase/genetics , Methylobacillus/enzymology , Methylobacillus/genetics , Cloning, Molecular , DNA, Bacterial/biosynthesis , DNA, Bacterial/genetics , Databases, Genetic , Flavin-Adenine Dinucleotide/metabolism , Molecular Weight , Molybdenum/metabolism , Sequence Analysis, Protein , Xanthine Oxidase/chemistry , Xanthine Oxidase/geneticsABSTRACT
In order to establish an efficient process to decompose environmentally toxic aldehydes, dioxygen-dependent aldehyde oxidase (ALOD) from microorganisms was first sought, and some bacteria and actinomycetes were found to produce the enzyme in their cells. Methylobacillus sp., Pseudomonas sp. and Streptomyces moderates were selected as the representative ALOD-producing strains and their enzymes were partially purified and characterized. The three ALODs could oxidize a wide range of aldehydes including formaldehyde, aliphatic aldehydes, and aromatic aldehydes, though their preferences differ depending on their producing strains. The other enzymatic properties were also determined with regard to their producing strains. Methylobacillus sp. ALOD had the most acidic optimum pH for its activity and stability and Pseudomonas sp. ALOD had the highest stability against heat treatment. Three native ALODs had molecular weights ranging from 140 to 148 kDa and were composed of three subunits of different sizes: large (85 to 88 kDa), medium-sized (37 to 39 kDa) and small (18 to 23 kDa).