Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from <i>Proteus mirabilis</i>

Shanshan Pei; Xiaobo Ruan; Jia Liu; Wei Song; Xiulai Chen; Qiuling Luo; Liming Liu; Jing Wu

Your Location：

Home >

Browse articles >

Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis

Biotechnology and Bioengineering | Updated：2026-01-06

- Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis
- Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis
- 中国化学工程学报（英文版） 2020年28卷第8期页码：2190-2199
- Affiliations：
  
  1. School of Pharmaceutical Science, Jiangnan University,Wuxi,China,214122
  2. Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University,Wuxi,China,214122
  3. State Key Laboratory of Food Science and Technology, Jiangnan University,Wuxi,China,214122
  4. National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University,Wuxi,China,214122
- Author bio：
- Funds：
- DOI：
  中图分类号：
- 纸质出版：2020
- Accepted：
Scan QR Code
Shanshan Pei, Xiaobo Ruan, Jia Liu, 等. Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis[J]. 中国化学工程学报（英文版）, 2020,28(8):2190-2199.

[J]. 中国化学工程学报, 2020, 28(8): 2190-2199.
Shanshan Pei, Xiaobo Ruan, Jia Liu, 等. Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis[J]. 中国化学工程学报（英文版）, 2020,28(8):2190-2199. DOI：

[J]. 中国化学工程学报, 2020, 28(8): 2190-2199. DOI：

摘要

Abstract

L-Amino acid deaminase (LAAD) is a key enzyme in the deamination of L-valine (L-val) to produce α- ketoisovalerate (KIV). However

the product inhibition of LAAD is a major hindrance to industrial KIV production. In the present study

a combination strategy of modification of flexible loop regions around the product binding site and the avoidance of dramatic change of main-chain dynamics was reported to reduce the product inhibition. The four mutant PM-LAAD

(PM-LAAD

S98A/T105A/S106A/L341A

) achieved a 6.2-fold higher catalytic efficiency and an almost 6.7-fold reduction in product inhibition than the wild-type enzyme. Docking experiments suggested that weakened interactions between the product and enzyme

and the flexibility of the “lid” structure relieved LAAD product inhibition. Finally

the whole-cell biocatalyst PM-LAAD

has been applied to KIV production

the titer and conversion rate of KIV from L-val were 98.5 g·L

-1

and 99.2% at a 3-L scale

respectively. These results demonstrate that the newly engineered catalyst can significantly reduce the product inhibition

that making KIV a prospective product by bio

conversion method

and also provide the understanding of the mechanism of the relieved product inhibition of PM-LAAD.

关键词

Keywords

references

浏览量

142

Downloads

CSCD

文章被引用时，请邮件提醒。

Submit

工具集

关联资源

Recent advances in microbial production of phenolic compounds

Enhanced mass transfer in flexible electrodes of open-pore cobalt disulfide nanosheets supported on sulfur-doped carbon fibers for efficient zinc-air batteries

The melting transformation mechanism of corundum and mullite in coal ash under reducing atmosphere

Synergistically coupling of vertically oriented Ru/Co co-doped MoS2 with interfacial engineering for efficient electrochemical hydrogen evolution

Nano-confinement construction of FeCo@NCNTs nanocomposite for pH-universal oxygen reduction catalysis and high-power Zn-air battery

Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis

Enhancement of α-ketoisovalerate production by relieving the product inhibition of L-amino acid deaminase from Proteus mirabilis

DOI：

摘要

Abstract

关键词

Keywords

references