...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Phycobilin: cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins
【24h】

Phycobilin: cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins

机译：藻胆素：半胱氨酸-84胆汁蛋白裂解酶，是一种蓝藻藻胆蛋白中半胱氨酸-84结合位点的近乎通用的裂解酶

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

Phycobilisomes, the light-harvesting complexes of cyanobacteria and red algae, contain two to four types of chromophores that are attached covalently to seven or more members of a family of homologous proteins, each carrying one to four binding sites. Chromophore binding to apoproteins is catalyzed by lyases, of which only few have been characterized in detail. The situation is complicated by nonen-zymatic background binding to some apoproteins. Using a modular multiplasmidic expression-reconstitution assay in Escherichia coli with low background binding, phycobilin:cystein-84 biliprotein lyase (CpeS1) from Anabaena PCC7120, has been characterized as a nearly universal lyase for the cysteine-84-binding site that is conserved in all biliproteins. It catalyzes covalent attachment of phycocyanobilin to all allophycocyanin subunits and to cysteine-84 in the β-subunits of C-phycocyanin and phycoerythrocyanin. Together with the known lyases, it can thereby account for chromophore binding to all binding sites of the phycobiliproteins of Anabaena PCC7120. Moreover, it catalyzes the attachment of phycoerythrobilin to cysteine-84 of both subunits of C-phycoerythrin. The only exceptions not served by CpeS1 among the cysteine-84 sites are the α-subunits from phycocyanin and phycoerythrocyanin, which, by sequence analyses, have been defined as members of a subclass that is served by the more specialized E/F type lyases.
机译：藻胆体是蓝细菌和红藻的光捕获复合物，包含两到四种类型的生色团，它们共价连接到一个或多个同源蛋白家族的七个或更多成员上，每个成员带有一个到四个结合位点。发色团与脱辅基蛋白的结合是由裂解酶催化的，其中只有很少的特征。非酶背景与某些载脂蛋白的结合使情况复杂化。使用具有低背景结合力的大肠杆菌中的模块化多质粒表达-重组测定法，来自Anabaena PCC7120的藻胆素：半胱氨酸-84胆汁蛋白裂解酶（CpeS1）被表征为保守的半胱氨酸84结合位点的近乎通用裂解酶所有胆蛋白。它催化藻蓝蛋白共价附于所有藻蓝蛋白亚基以及C-藻蓝蛋白和藻红蛋白β-亚基中的半胱氨酸84。它与已知的裂解酶一起可以解释发色团与鱼腥藻PCC7120藻胆蛋白的所有结合位点的结合。此外，它催化藻红蛋白结合到C-藻红蛋白两个亚基的半胱氨酸84上。在半胱氨酸84位点中，CpeS1唯一不提供的例外是藻蓝蛋白和藻红蛋白的α亚基，通过序列分析，它们被定义为由更专业的E / F型裂解酶提供服务的亚类成员。

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