Aldehyde oxidase carrying an unusual subunit structure from Pseudomonas sp. MX-058.
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.
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Rungruedee
R
Thiwthong
Michihiko
M
Kataoka
Akira
A
Iwasaki
Hiroshi
H
Watanabe
Junzo
J
Hasegawa
Kimiyasu
K
Isobe
Sakayu
S
Shimizu
D042931:Aldehyde Oxidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D004795:Enzyme Stability; D007700:Kinetics; D008969:Molecular Sequence Data; D021122:Protein Subunits / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011549:Pseudomonas / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
D021122:Protein Subunits; D042931:Aldehyde Oxidase
Gene. 1995 Dec 29;167(1-2):215-9
8566780
Anal Biochem. 1976 May 7;72:248-54
942051
Eur J Biochem. 2000 Jan;267(1):3-10
10601844
Mol Biotechnol. 2003 Nov;25(3):207-14
14668534
Appl Microbiol Biotechnol. 2005 Jul;68(1):53-6
15657722
J Biol Chem. 1997 Jun 13;272(24):15280-5
9182554
Biosci Biotechnol Biochem. 1995 Apr;59(4):576-81
7772820
J Mol Biol. 1971 Dec 28;62(3):465-77
5136579
FEMS Microbiol Lett. 2003 Dec 5;229(1):31-6
14659539
J Biosci Bioeng. 2002;94(2):124-9
16233281
Bioorg Med Chem. 1994 Jun;2(6):371-8
8000856
J Biol Chem. 1995 Dec 29;270(52):31037-45
8537361
Appl Environ Microbiol. 1983 May;45(5):1582-5
6870241