Superoxide dismutases exhibit oxidase activity on aldehyde alcohols similar to alcohol oxidase from Paenibacillus sp. AIU 311.
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 (Mn(2+)-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 Mn(2+)-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 Mn(2+)-SOD were classified into a similar group.
Isobe
Kimiyasu
K
Department of Agro-bioscience, Iwate University, Morioka, Japan. kiso@iwate-u.ac.jp
Kato
Ayako
A
Sasaki
Yasutaka
Y
Kataoka
Michihiko
M
Ogawa
Jun
J
Iwasaki
Akira
A
Hasegawa
Junzo
J
Shimizu
Sakayu
S
D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D001406:Bacillaceae / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D013482:Superoxide Dismutase / Q000737:chemistry*
D000429:Alcohol Oxidoreductases; C019643:alcohol oxidase; D013482:Superoxide Dismutase