The lid domain in lipases: Structural and functional determinant of enzymatic properties

Faez Iqbal Khan, Dongming Lan, Rabia Durrani, Weiqian Huan, Zexin Zhao, Yonghua Wang*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

273 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article number16
JournalFrontiers in Bioengineering and Biotechnology
Volume5
Issue numberMAR
DOIs
Publication statusPublished - 9 Mar 2017
Externally publishedYes

Keywords

  • Interfacial activation
  • Lid domain
  • Lipase
  • Protein engineering
  • Thermostability

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