Molecular directionality in polysaccharide synthesis by glucosyltransferase
Molecular directionality in polysaccharide synthesis by glucosyltransferase
批准号:
12660151
负责人:
SUGIYAMA Junji
金额:
$2.62万
依托单位:
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
项目状态:
已结题
起止时间:
2000 至 2001
中文摘要
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英文摘要
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.
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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)
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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.
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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。
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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。
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Imai et al.: "Directional degradation of β-chitin by chitinase A1 revealed by a novel reducing end labelling technique"FEBS Lett.. 510. 201-205 (2002)
Imai 等人:“通过新颖的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 Lett.. 510. 201-205 (2002)
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