• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>IUBMB life >Site-directed mutagenesis of Asp313, Glu315, and Asp391 residues in Chitinase of Aeromonas Caviae
【24h】

Site-directed mutagenesis of Asp313, Glu315, and Asp391 residues in Chitinase of Aeromonas Caviae

机译：Caviae几丁质酶几丁质酶中Asp313，Glu315和Asp391残基的定点诱变

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Site-directed mutagenesis was used to explore the roles of amino acid residues involved in the activity of chitinase from Aeromonas caviae. Kinetic parameters for 4-methylumbelliferyl-N,N'-diacetylchitobiose or 4-methylumbelliferyl-N,N',N".triacetylchitotriose hydrolysis were determined with wild-type and mutant chitinases. Chitinases with the mutations E315D (or Q) and D391E (or N) were severely impaired and had dramatically decreased k_(cat). However, the effect of the these mutations on the K_m values were different. The function of the carboxyl group of Asp313 was partially replaced by the amide of Asn when the 4-methylumbelliferyl-N,N',N".triace. tylchitotriose substrate was used. Results indicated that Asp313, Glu315, and Asp391 might be the best candidates for the catalytic residues of chitinase A from Aeromonas caviae.
机译：使用定点诱变来探讨氨基酸残基参与来自豚鼠气单胞菌的几丁质酶活性的作用。用野生型和突变型几丁质酶测定4-甲基伞形基-N，N'-二乙酰基壳二糖或4-甲基伞形基-N，N'，N”。三乙酰基壳三糖水解的动力学参数。具有突变E315D（或Q）和D391E（或N）受到严重损害，并且k_（cat）显着降低，但是这些突变对K_m值的影响不同，Asp313的羧基部分被Asn的酰胺所取代，当4-甲基伞形酮基-N，N'，N“ .triace。使用了叔丁基三糖底物。结果表明，Asp313，Glu315和Asp391可能是猪气单胞菌几丁质酶A催化残基的最佳候选者。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号