Purification and characterization of a novel alcohol oxidase from Paenibacillus sp. AIU 311.
An oxidase catalyzing the conversion of glycolaldehyde to glyoxal was purified to the homogeneous state from Paenibacillus sp. AIU 311, and its properties were revealed. This enzyme was specific to glycolaldehyde and glyceraldehyde, and the reaction rates to other alcohols and aldehydes were less than 6% of that of glycolaldehyde. The Km values for glycolaldehyde and glyceraldehyde were estimated to be 13.2 and 7.5 mM, respectively. The glycolaldehyde oxidation was optimum at pH 6.5 and 50 degrees C. The molecular mass of this enzyme was 49 kDa, and it consisted of two identical subunits of 24 kDa. The NH2-terminal sequence was not homologous to those of alcohol oxidases. This is the first report of an oxidase exhibiting high specificity to a hydroxy group of aldehyde alcohols.
Isobe
Kimiyasu
K
Department of Agro-bioscience, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan. kiso@iwate-u.ac.jp
Kato
Ayako
A
Sasaki
Yasutaka
Y
Suzuki
Shuuya
S
Kataoka
Michihiko
M
Ogawa
Jun
J
Iwasaki
Akira
A
Hasegawa
Junzo
J
Shimizu
Sakayu
S
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D001407:Bacillus / Q000145:classification* / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D013045:Species Specificity; D013379:Substrate Specificity
D000429:Alcohol Oxidoreductases; C019643:alcohol oxidase