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

Thiwthong R, Kataoka M, Iwasaki A, Watanabe H, Hasegawa J, Isobe K, Shimizu S - Microb Biotechnol (2008)

Bottom Line: All of these homologous oxidoreductases have a heterotrimer structure consisting of 85-88 (α), 37-39 (β) and 18-23 (γ) kDa subunits.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.

View Article: PubMed Central - PubMed

Affiliation: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.

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Substrate specificity of aldehyde oxidases (F10 and F13) from Pseudomonas sp. MX‐058. Reactions were carried out under the standard conditions and the activity is expressed relative to that toward glyoxal taken as 100%.
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f5: Substrate specificity of aldehyde oxidases (F10 and F13) from Pseudomonas sp. MX‐058. Reactions were carried out under the standard conditions and the activity is expressed relative to that toward glyoxal taken as 100%.

Mentions: The oxidizing activity of the two fractions toward various substrates including aliphatic aldehydes, aromatic aldehydes, glyoxylic acid, glycolic acid, xanthine and hypoxanthine was examined (Fig. 5). Neither fraction showed any activity toward xanthine or hypoxanthine (a substrate for xanthine oxidase, E.C 1.1.3.22), or glycolic acid (a substrate for glycolate oxidase, EC 1.1.3.15), indicating that they did not have xanthine oxidase or glycolate oxidase activity respectively. Both F10 and F13 showed high activity toward aliphatic aldehydes and aromatic aldehydes, preferentially benzaldehyde, and showed essentially the same substrate specificity profile. An advantageous property for glyoxylic acid production from glyoxal with aldehyde oxidases F10 and F13 was the significantly low activity toward glyoxylic acid compared with glyoxal.


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

Thiwthong R, Kataoka M, Iwasaki A, Watanabe H, Hasegawa J, Isobe K, Shimizu S - Microb Biotechnol (2008)

Substrate specificity of aldehyde oxidases (F10 and F13) from Pseudomonas sp. MX‐058. Reactions were carried out under the standard conditions and the activity is expressed relative to that toward glyoxal taken as 100%.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3815246&req=5

f5: Substrate specificity of aldehyde oxidases (F10 and F13) from Pseudomonas sp. MX‐058. Reactions were carried out under the standard conditions and the activity is expressed relative to that toward glyoxal taken as 100%.
Mentions: The oxidizing activity of the two fractions toward various substrates including aliphatic aldehydes, aromatic aldehydes, glyoxylic acid, glycolic acid, xanthine and hypoxanthine was examined (Fig. 5). Neither fraction showed any activity toward xanthine or hypoxanthine (a substrate for xanthine oxidase, E.C 1.1.3.22), or glycolic acid (a substrate for glycolate oxidase, EC 1.1.3.15), indicating that they did not have xanthine oxidase or glycolate oxidase activity respectively. Both F10 and F13 showed high activity toward aliphatic aldehydes and aromatic aldehydes, preferentially benzaldehyde, and showed essentially the same substrate specificity profile. An advantageous property for glyoxylic acid production from glyoxal with aldehyde oxidases F10 and F13 was the significantly low activity toward glyoxylic acid compared with glyoxal.

Bottom Line: All of these homologous oxidoreductases have a heterotrimer structure consisting of 85-88 (α), 37-39 (β) and 18-23 (γ) kDa subunits.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.

View Article: PubMed Central - PubMed

Affiliation: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.

Show MeSH
Related in: MedlinePlus