Molecular directionality in polysaccharide synthesis by glucosyltransferase

葡萄糖基转移酶合成多糖的分子方向性

• 批准号: 12660151
• 负责人: SUGIYAMA Junji
• 金额: $ 2.62万
• 依托单位: KYOTO UNIVERSITY
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 2000
• 资助国家: 日本
• 起止时间: 2000 至 2001
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-12660151/
• 关键词: reducing end; cellulose; hemicellulose; reductive amination; biotin-streptaridin reaction; parallel packing; antiparallel packing; キチン

We have developed a recipe for labeling reducing end of polysaccharide chains by reductive amination for microscopic visualization by TEM. This method was applied to investigate the following topics,1. Structure of native microfibrils and their directionality of synthesis.2. Chain packing in cellulose and chitin polymorphs3. Molecular directionality of enzymatic degradation4. Preference in binding modules of some cellobiohydrolases.1. The "parallel-up" structure was confirmed both for cellulose I and β-chitin. The polymerization of those chains was found to occur at non-reducing ends.2. Cellulose III was parallel while II was anti-parallel, which are in good accord with the previous studies on these polymorphs. However, the reducing end labeling of α-chitin was not in good accord with anti-parallel structure.3. Chitinase A and B from Serratia was found to digest b-chitin microfibrils from their reducing ends and non-reducing ends, respectively.4. Binding modules from some cellobiohydrolases showed preferential adsorption to the hydrophobic surface of cellulose : i.e. (100) surface of cellulose crystals.

我们通过还原氨的标记，用于将微观可视化的末端用于研究以下主题。 l-up的结构已确认纤维素I和β-智力素。发现这些链的聚合发生在非还原末端。与抗平行结构的良好相吻。3从还原和非还原末端产生了来自Serratia的几丁质酶A和B。 。

项目成果

Imai: "Directional degradation of β-chitin by chitinase A1 revealed by a novel reducing end labeling technique"FEBS Letters 510. 201. 201-205 (2002)

今井：“新型还原末端标记技术揭示了几丁质酶 A1 对 β-几丁质的定向降解”FEBS Letters 510. 201. 201-205 (2002)

Uchiyama et al.: "Roles of the exposed aromatic residues in Crystalline chitin hydrolysis by chitinase A from Serratia Marcescens 2170"J. Biol. Chem.. 276. 41343-41349 (2001)

Uchiyama 等人：“粘质沙雷氏菌 2170 的几丁质酶 A 水解结晶几丁质中暴露的芳香族残基的作用”J.

Yamanaka et al.: "Structrural modification of bacterial cellulose"Cellulose. 7. 213-225 (2000)

Yamanaka 等人：“细菌纤维素的结构修饰”纤维素。

Uchiyama: "Roles of the Exposed Aromatic Residues in Crystalline Chitin Hydrolysis by Chitinase A from Serratia marcescens 2170^*"J. Biol. Chem.. 276. 41343-41349 (2001)

Uchiyama：“粘质沙雷氏菌 2170^* 的几丁质酶 A 水解结晶几丁质中暴露的芳香残基的作用”J。

Wada et al.: "Improved structural data of cellulose III1 prepared in supercritical ammonia"Macromorecules. 34. 1237-1243 (2001)

Wada 等人：“改进了在超临界氨中制备的纤维素 III1 的结构数据”Macromorecules。