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キムラ マサヒロ
木村 将大 所属 応用生物学部 応用生物学科 職種 助教 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2017/08 |
| 形態種別 | 学術論文 |
| 査読 | 査読あり |
| 標題 | Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH. |
| 執筆形態 | 共著 |
| 掲載誌名 | FEBS Letters |
| 掲載区分 | 国外 |
| 出版社・発行元 | Wiley / FEBS Press |
| 巻・号・頁 | 591(20),pp.3310-3318 |
| 著者・共著者 | Wakita, S., Kobayashi, S., Kimura, M., Kashimura, A., Honda, S., Sakaguchi, M., Sugahara, Y., Kamaya, M., Matoska, V., Bauer, PO., and Oyama, F |
| 概要 | Mouse acidic mammalian chitinase (AMCase) degrades chitin with highest efficiency at pH 2.0 and is active up to pH 8.0. Here, we report that mouse AMCase also exhibits transglycosylation activity under neutral conditions. We incubated natural and artificial chitin substrates with mouse AMCase at pH 2.0 or 7.0 and analyzed the resulting oligomers using an improved method of fluorescence-assisted carbohydrate electrophoresis. Mouse AMCase produces primarily dimers of N-acetyl-d-glucosamine [(GlcNAc)2 ] under both pH conditions while generating transglycosylated (GlcNAc)3 primarily at pH 7.0 and at lower levels at pH 2.0. These results indicate that mouse AMCase catalyzes hydrolysis as well as transglycosylation and suggest that this enzyme can play a novel role under physiological conditions in peripheral tissues, such as the lungs. |
| 外部リンクURL | https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.12798 |