VD_3羟基化酶的定向研究进展  

Advances in Directed Research of VD_3 Hydroxylase

作　　者：刘苗[1] 汪永辉[1] 陆群[1] 

机构地区：[1]西南交通大学生命科学与工程学院,成都610031

出　　处：《生物技术通报》2014年第1期27-31,共5页Biotechnology Bulletin

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。采用定向构建Vdh重组质粒的方法对Vdh催化活性位点给予优化,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。Vitamin D3 hydroxylase is a cytochrome P450 （ CYP ） responsible for the biocatalytic conversion of vitamin D3 to la, 25- dihydroxyvitamin D3 （ la, 25 （ OH ）2VD3 ）o 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.

关 键 词：Vdh异源表达氧化还原蛋白定向突变25(OH)VD3 LA 25(OH)2VD3 

分 类 号：Q814[生物学—生物工程]