Construction of fusion protein systems consisting of a chiral alcohol dehydrogenase and a formate dehydrogenase

WU Xi; ZHANG Chong; XING Xinhui

您当前的位置：

首页 >

文章列表页 >

Construction of fusion protein systems consisting of a chiral alcohol dehydrogenase and a formate dehydrogenase

更新时间：2025-12-10

- Construction of fusion protein systems consisting of a chiral alcohol dehydrogenase and a formate dehydrogenase
- CIESC Journal Issue 10, Pages: 2562-2567(2009)
- 作者机构：
  
  清华大学化学工程系
- 作者简介：
- 基金信息：
- DOI：
  CLC：
- Online First：05 October 2009，
  
  Published：05 October 2009
- 稿件说明：
移动端阅览
WU Xi, ZHANG Chong, XING Xinhui. Construction of fusion protein systems consisting of a chiral alcohol dehydrogenase and a formate dehydrogenase[J]. CIESC Journal, 2009, (10): 2562-2567.
DOI：

WU Xi, ZHANG Chong, XING Xinhui. Construction of fusion protein systems consisting of a chiral alcohol dehydrogenase and a formate dehydrogenase[J]. CIESC Journal, 2009, (10): 2562-2567. DOI：

摘要

为了在手性催化的同时实现辅酶的再生，利用源于红平红球菌Rhodococcus erythropolis的手性醇脱氢酶chiral alcohol dehydrogenase(READH)与来源于博伊丁假丝酵母Candida boidinii的甲酸脱氢酶formate dehydrogenase(CbFDH)构建了一系列具有双酶活性的融合蛋白体系。分别为：1）READH的N端与麦芽糖结合蛋白maltose binding protein(MBP)的C端融合；2）CbFDH的N端与MBP的C端融合；3）READH的N端与CbFDH的C端融合；4）READH的C端与CbFDH的N端融合。结果表明：在所有的融合策略中，READH的活性都受到了较大的影响。READH在N端融合在CbFDH的C端后活性最高，但是此时CbFDH不具有活性。相反，READH的C端与CbFDH的N端融合后，CbFDH具有最高的活性。在READH的C端与CbFDH的N端融合的策略下，两者都具有活性。表明通过合理设计具有双重功能的融合蛋白，有望能提高其催化效率，为新型辅酶再生系统的建立提供基础。

Abstract

The bifunctional fusion protein systems consisting of Rhodococcus erythropolis chiral alcohol dehydrogenase (READH)

Candida boidinii formate dehydrogenase (CbFDH) or maltose binding protein (MBP) were constructed to regenerate the cofactors for biocatalysis.READH originated from Rhodococcus erythropolis is an (S)-specific nicotinamide adenine dinucleotide (NADH)dependent alcohol dehydrogenase

meanwhile

CbFDH originated from Candida boidinii is an NADH-dependent formate dehydrogenaseThe strategies of the different fusion protein systems included: (1) fusion of the N terminus of READH to the C terminus of MBP

(2) fusion of the N terminus of CbFDH to the C terminus of MBP

(3) fusion of the N terminus of READH to the C terminus of CbFDH

(4) fusion of the C terminus of READH to the N terminus of CbFDHThe activities of READHs were depressed in all fusion strategiesWhen the N terminus of READH was fused to the C terminus of CbFDH

READH reached the highest activity

but CbFDH had no activity.In contrast

when the C terminus of READH was fused to the N terminus of CbFDH

CbFDH showed the highest activity

and both moieties displayed activities.From this study

the authors suggest that the rational design of the bifunctional fusion protein system may improve the biocatalysis efficiency by the simultaneous cofactor regeneration.

关键词

Keywords

references

Views

301

下载量

CSCD

Alert me when the article has been cited

提交

Tools

Publicity Resources

Exothermic characteristics of energy carrier for calcium looping thermo-chemical energy storage

Oxygen mass transfer performance of hollow fiber non-bubble aeration membrane based on gas/liquid-phase measurement method

Study on microwave enhanced removal performance of organic matter in coking waste salt

Recent advances and perspectives on sulfide-based photocatalysts for hydrogen production

Methods of adaptive prediction and abnormal states traceability for sulphur content in flue gas desulfurization process

Related Author

No data

Related Institution

No data

⁰