生物技术通报 ›› 2014, Vol. 0 ›› Issue (1): 27-31.

• 综述与专论 • 上一篇    下一篇

VD3 羟基化酶的定向研究进展

刘苗,汪永辉,陆群   

  1. 西南交通大学生命科学与工程学院,成都 610031
  • 收稿日期:2013-08-09 出版日期:2014-01-23 发布日期:2014-01-23
  • 作者简介:刘苗, 女, 硕士研究生, 研究方向: 生物转化;E-mail: 920946828@qq.com

Advances in Directed Research of VD3 Hydroxylase

Liu Miao, Wang Yonghui, Lu Qun   

  1. School of Life Science and Engineering of Southwest Jiaotong Uiversity,Chengdu 610031
  • Received:2013-08-09 Published:2014-01-23 Online:2014-01-23

摘要: 维生素D3 羟基化酶(Vdh) 作为细胞色素酶P450s(CYP) 蛋白家族成员,催化VD3 形成有生物活性#br#的1α,25(OH)2VD3。但是,由于VD3 并不是Vdh 的天然底物,Vdh 羟基化活性较低。采用定向#br#构建Vdh 重组质粒的方法对Vdh 催化活性位点给#br#予优化,从而提高其羟基化能力。就目前对Vdh 的结构特性和定向研究进行综述。

关键词: Vdh 异源表达, 氧化还原蛋白, 定向突变, 25(OH)VD3 1α, 25(OH)2VD3

Abstract: Vitamin D3 hydroxylase is a cytochrome P450(CYP)responsible for the biocatalytic conversion of vitamin D3 to 1α, 25dihydroxyvitamin D3(1α, 25(OH)2VD3)。Since VD3 is not a natural substrate for Vdh, the hydroxylase of Vdh is quite low. Researchers construct a novel of recombination Vdh plasmid by directed evolution to optimize the active sites of catalytic structure, thereby improving the hydroxylase ability. This article reviewed Vdh structure properties and development of directed evolution.

Key words: Vdh Heterologous expression, Redox partner protein, Directed evolution, 25-hydroxyvitaminD3 1α, 25- dihyroxyvitamin D3