首页> 外文会议>日本化学会春季年会講演予稿集 >Enhanced peroxidase activity of hexameric tyrosine-coordinated hemoprotein by substitution of an amino acid residue axially ligating to the heme molecule
【24h】

Enhanced peroxidase activity of hexameric tyrosine-coordinated hemoprotein by substitution of an amino acid residue axially ligating to the heme molecule

机译:通过从轴向连接到血红素分子的氨基酸残基取代氨基酸残基来增强过氧化物酶活性的六氧化酪氨酸配位的血蛋白

获取原文

摘要

Hexameric tyrosine-coordinated heme protein, HTHP, is a thermally stable homohexamer, which contains a tyrosine-coordinated heme cofactor in each subunit. Although the function of HTHP is still unknown, the rigid and highly-symmetric structure could be useful materials for a newly-engineered protein.1
机译:六聚酪氨酸配位血红素蛋白,HTHP是热稳定的同源物,其在每个亚基中含有酪氨酸配位的血红蛋白。虽然HTHP的功能仍然未知,但刚性和高度对称的结构可能是新工程化蛋白的有用材料

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