Intracellular substrates of a heme-containing ascorbate oxidase in Pleurotus ostreatus

A novel heme-containing ascorbate oxidase isolated from oyster mushroom, Pleurotus ostreatus, catalyzes oxidation of ascorbic acid (Kim et al., 1996). In this report, we describe the identification of intracellular substrates of the enzyme in the mushroom. Six compounds, which can serve as substrate...

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Published inThe journal of microbiology Vol. 47; no. 2; pp. 178 - 186
Main Authors Lee, S.R. (Chonnam National University Medical School, Gwangju, Republic of Korea), E-mail: leesr@chonnam.ac.kr, Joo, W.J. (Seoul National University, Seoul, Republic of Korea), Baek, Y.U. (Seoul National University, Seoul, Republic of Korea), Lee, Y.K. (Seoul National University, Seoul, Republic of Korea), Yu, S.W. (Seoul National University, Seoul, Republic of Korea), Kim, Y.R. (Seoul National University, Seoul, Republic of Korea), Chay, K.O. (Chonnam National University Medical School, Gwangju, Republic of Korea), Cho, S.H. (Seoul National University, Seoul, Republic of Korea), Kang, S.O. (Seoul National University, Seoul, Republic of Korea), E-mail: kangsaou@snu.ac.kr
Format Journal Article
LanguageEnglish
Published Heidelberg The Microbiological Society of Korea 01.04.2009
Springer Nature B.V
한국미생물학회
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Summary:A novel heme-containing ascorbate oxidase isolated from oyster mushroom, Pleurotus ostreatus, catalyzes oxidation of ascorbic acid (Kim et al., 1996). In this report, we describe the identification of intracellular substrates of the enzyme in the mushroom. Six compounds, which can serve as substrate of the heme-containing ascorbate oxidase, were identified as L-ascorbic acid, D-erythroascorbic acid, 5-O-(α-D-glucopyranosyl)-D-erythroascorbic acid, 5-O-(α-D-xylopyranosyl)-D-erythroascorbic acid, 5-methyl-5-O-(α-D-glucopyranosyl)-D-erythroascorbic acid, and 5-methyl-5-O-(α-D-xylopyranosyl)-D-erythroascorbic acid. All of the compounds were oxidized at a significant rate by the heme-containing ascorbate oxidase. Oxidation of the compounds produced equimolar amounts of hydrogen peroxide per mole of substrate.
Bibliography:A50
2009004702
ObjectType-Article-1
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http://msk.jams.or.kr/jams/co/download/popup/poDownload.kci?storFileBean.orteFileId=FI0002204357
G704-000121.2009.47.2.006
ISSN:1225-8873
1976-3794
DOI:10.1007/s12275-008-0307-8