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シュードモナス細菌のイソアミラーゼとマルトテトラオース生成アミラーゼの一次構造と遺伝子発現
https://fukuyama-u.repo.nii.ac.jp/records/7781
https://fukuyama-u.repo.nii.ac.jp/records/778193be6808-963d-4bf0-94f4-36f1d26bc6ea
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
KJ00005781160.pdf (1.2 MB)
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| Item type | 紀要論文(ELS) / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 1990-01-01 | |||||
| タイトル | ||||||
| タイトル | シュードモナス細菌のイソアミラーゼとマルトテトラオース生成アミラーゼの一次構造と遺伝子発現 | |||||
| タイトル | ||||||
| タイトル | Primary Structures and Gene Expressions of Pseudomonas Isoamylase and Maltotetraose-Forming Amylase | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | jpn | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Pseudomonas | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Isoamylase | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | Maltotetraose-forming amylase | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | departmental bulletin paper | |||||
| ページ属性 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | P(論文) | |||||
| 著者名(日) |
藤田, 昌也
× 藤田, 昌也 |
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| 著者名よみ | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 41967 | |||||
| 姓名 | フジタ, マサヤ | |||||
| 著者名(英) | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 41968 | |||||
| 姓名 | FUJITA, Masaya | |||||
| 言語 | en | |||||
| 著者所属(日) | ||||||
| 値 | 福山大学工学部生物工学科 | |||||
| 抄録(英) | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | Isoamylase and maltotetraose-forming amylase (G_4-amylase) produced by Pseudomonas are important enzymes in the starch industry. The isoamylase hydrolyzes branching points with α-1,6-glucosidic linkages in amylopectin and glycogen, and produces linear maltodextrins. The G_4-amylase catalyzes the release of α-maltotetraose exoglycolytically from the nonreducing ends of starch, whereas other exo-type amylases (glucoamylase and β-amylase) release β-anomeric products by exoglycolytic cleavage, and α-amylase hydrolyzes starch endoglycolytically to produce α-malto-oligosaccharides. Thus, the G_4-amylase has unique activity for hydrolysis of starch intermediate between those of α-amylase and β-or glucoamylase. For understanding the molecular basis of the unique action mechanism of isoamylase and G_4-amylase and also for elucidating the regulation of the syntheses of these enzymes, we determined the nucleotide sequences of these genes and examined the regulation of these gene expressions. The isoamylase was consisted of 771 amino acids which contained 26 residues as a signal peptide. The G_4-amylase was consisted of 547 amino acids which contained 21 residues as a signal peptide. These two amylases contained four sequences conserved in many other amylases. These four sequences probably form a cleft involved in catalytic function and substrate binding. Expressions of the isoamylase gene (iam) and the G_4-amylase gene (amyP) were induced by maltose. The expression of the latter was repressed by glucose at posttranscriptional level, whereas that of the former was not repressed by glucose. | |||||
| 雑誌書誌ID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AN00217655 | |||||
| 書誌情報 |
福山大学工学部紀要 巻 12, p. 189-200, 発行日 1990 |
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