Open AccessAldehyde oxidase carrying an unusual subunit structure from Pseudomonas sp. MX‐058
Author(s) -
Thiwthong Rungruedee,
Kataoka Michihiko,
Iwasaki Akira,
Watanabe Hiroshi,
Hasegawa Junzo,
Isobe Kimiyasu,
Shimizu Sakayu
Publication year - 2008
Publication title -
microbial biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.287
H-Index - 74
ISSN - 1751-7915
DOI - 10.1111/j.1751-7915.2008.00038.x
Subject(s) - heterotetramer , glyoxylic acid , biochemistry , glyoxal , aldehyde oxidase , aldehyde , protein subunit , chemistry , amino acid , stereochemistry , enzyme , organic chemistry , catalysis , gene , xanthine oxidase
Summary 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 (α), 37‐39 (β) and 18‐23 (γ) kDa subunits. However, the α‐subunits of F10 and F13 might have decomposed into two [80 (α 1 ) and 9 kDa (α 2 )] and three [58 (α 1′ ), 22 (α 1″ ) and 9 (α 2 ) kDa] subunits, respectively, while the β‐ and γ‐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, α 1 α 2 βγ for F10 and α 1′ α 1″ α 2 βγ 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.