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Superoxide dismutases exhibit oxidase activity on aldehyde alcohols similar to alcohol oxidase from Paenibacillus sp. AIU 311

Paper ID Volume ID Publish Year Pages File Format Full-Text
22400 43274 2008 5 PDF Available
Title
Superoxide dismutases exhibit oxidase activity on aldehyde alcohols similar to alcohol oxidase from Paenibacillus sp. AIU 311
Abstract

The relations between oxidase activity on aldehyde alcohols and superoxide dismutase (SOD) were investigated, since the amino terminal amino acid sequence of alcohol oxidase (AOD) from Paenibacillus sp. AIU 311, which was specific to aldehyde alcohols, exhibited high similarity to those of SODs containing manganese (Mn2+-SOD). Paenibacillus AOD had high SOD activity. The SODs containing manganese, iron, or copper and zinc also exhibited oxidase activities on aldehyde alcohols, and the relative values of oxidase activities on aldehyde alcohols to SOD activity of Mn2+-SOD were closer to those of Paenibacillus AOD compared with those of the other SODs. Thus, SODs had AOD activity on aldehyde alcohols as another enzyme activity, and the Paenibacillus AOD and Mn2+-SOD were classified into a similar group.

Keywords
glycolaldehyde; glyceraldehyde; alcohol oxidase; superoxide dismutase; Paenibacillus sp.
First Page Preview
Superoxide dismutases exhibit oxidase activity on aldehyde alcohols similar to alcohol oxidase from Paenibacillus sp. AIU 311
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 105, Issue 6, June 2008, Pages 666–670
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering