The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.
Lipases are important industrial enzymes. Most of the lipases operate at lipid-water interfaces enabled by a mobile lid domain located over the active site. Lid protects the active site and hence responsible for catalytic activity. In pure aqueous media, the lid is predominantly closed, whereas in the presence of a hydrophobic layer, it is partially opened. Hence, the lid controls the enzyme activity. In the present review, we have classified lipases into different groups based on the structure of lid domains. It has been observed that thermostable lipases contain larger lid domains with two or more helices, whereas mesophilic lipases tend to have smaller lids in the form of a loop or a helix. Recent developments in lipase engineering addressing the lid regions are critically reviewed here. After on, the dramatic changes in substrate selectivity, activity, and thermostability have been reported. Furthermore, improved computational models can now rationalize these observations by relating it to the mobility of the lid domain. In this contribution, we summarized and critically evaluated the most recent developments in experimental and computational research on lipase lids.
School of Food Science and Engineering, South China University of Technology, Guangzhou, China; School of Chemistry and Chemical Engineering, Henan University of Technology, Zhengzhou, China.
Faez Iqbal
FI
Khan
School of Food Science and Engineering, South China University of Technology , Guangzhou , China.
Dongming
D
Lan
School of Bioscience and Bioengineering, South China University of Technology , Guangzhou , China.
Rabia
R
Durrani
School of Bioscience and Bioengineering, South China University of Technology , Guangzhou , China.
Weiqian
W
Huan
School of Bioscience and Bioengineering, South China University of Technology , Guangzhou , China.
Zexin
Z
Zhao
School of Food Science and Engineering, South China University of Technology , Guangzhou , China.
Yonghua
Y
Wang
interfacial activation; lid domain; lipase; protein engineering; thermostability