A new aldehyde oxidase catalyzing the conversion of glycolaldehyde to glycolate from Burkholderia sp. AIU 129

• DOI: 10.1016/j.jbiosc.2014.09.005
• Publication Date: 2014-10-04T15:08:38Z
• Authors: Miwa Yamada; Keika Adachi; Natsumi Ogawa; Shigenobu Kishino; Jun Ogawa; Michihiko Kataoka; Sakayu Shimizu; Kimiyasu Isobe
• Keywords: Aldehydes; 0303 health sciences; Burkholderia; Xanthine Dehydrogenase; Temperature; Acetaldehyde; Hydrogen-Ion Concentration; Glycolates; Aldehyde Oxidase; Molecular Weight; Protein Subunits; 03 medical and health sciences; Metals; Biocatalysis; Amino Acid Sequence; Oxidation-Reduction

We found a new aldehyde oxidase (ALOD), which catalyzes the conversion of glycolaldehyde to glycolate, from Burkholderia sp. AIU 129. The enzyme further oxidized aliphatic aldehydes, an aromatic aldehyde, and glyoxal, but not glycolate or alcohols. The molecular mass of this enzyme was 130 kDa, and it was composed of three different subunits (αβγ structure), in which the α, β, and γ subunits were 76 kDa, 36 kDa, and 14 kDa, respectively. The N-terminal amino acid sequences of each subunit showed high similarity to those of putative subunits of xanthine dehydrogenase. Metals (copper, iron and molybdenum) and chelating reagents (α,α'-dipyridyl and 8-hydroxyquinoline) inhibited the ALOD activity. The ALOD showed highest activity at pH 6.0 and 50°C. Twenty mM glycolaldehyde was completely converted to glycolate by incubation at 30°C for 3 h, suggesting that the ALOD found in this study would be useful for enzymatic production of glycolate.