Aldehyde oxidase carrying an unusual subunit structure from Pseudomonas sp. MX-058.

ABSTRACT: Pseudomonas sp. MX-058 produces aldehyde oxidase catalysing glyoxal to glyoxylic acid. Two aldehyde oxidases (F10 and F13) were purified to homogeneity from Pseudomonas sp. MX-058. F10 and F13 had subunit structures, a heterotetramer and heteropentamer respectively. The N-terminal amino acid sequences of all subunits were highly homologous to amino acid sequences of the putative oxidoreductases of Pseudomonas strains. All of these homologous oxidoreductases have a heterotrimer structure consisting of 85-88 (?), 37-39 (?) and 18-23 (?) kDa subunits. However, the ?-subunits of F10 and F13 might have decomposed into two [80 (?(1)) and 9 kDa (?(2))] and three [58 (?(1')), 22 (?(1?)) and 9 (?(2)) kDa] subunits, respectively, while the ?- and ?-subunits remained intact. Both F10 and F13 show high activity toward several aliphatic and aromatic aldehydes. The aldehyde oxidases of Pseudomonas sp. MX-058 has unique protein structures, ?(1)?(2)?? for F10 and ?(1')?(1?)?(2)?? for F13, a heterotetramer and heteropentamer respectively. The enzymes exhibit significantly low activity toward glyoxylic acid compared with glyoxal, which is an advantageous property for glyoxylic acid production from glyoxal.

SUBMITTER: Thiwthong R 

PROVIDER: S-EPMC3815246 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature