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 t...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2017-03-01
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| Series: | Frontiers in Bioengineering and Biotechnology |
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| Online Access: | http://journal.frontiersin.org/article/10.3389/fbioe.2017.00016/full |
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| author | Faez Iqbal Khan Faez Iqbal Khan Dongming Lan Rabia Durrani Weiqian Huan Zexin Zhao Yonghua Wang |
| author_facet | Faez Iqbal Khan Faez Iqbal Khan Dongming Lan Rabia Durrani Weiqian Huan Zexin Zhao Yonghua Wang |
| author_sort | Faez Iqbal Khan |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-16T18:46:42Z |
| format | Article |
| id | doaj.art-ee0dcb214615461299483b7e2013efa7 |
| institution | Directory Open Access Journal |
| issn | 2296-4185 |
| language | English |
| last_indexed | 2024-12-16T18:46:42Z |
| publishDate | 2017-03-01 |
| publisher | Frontiers Media S.A. |
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| series | Frontiers in Bioengineering and Biotechnology |
| spelling | doaj.art-ee0dcb214615461299483b7e2013efa72022-12-21T22:20:49ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852017-03-01510.3389/fbioe.2017.00016247303The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic PropertiesFaez Iqbal Khan0Faez Iqbal Khan1Dongming Lan2Rabia Durrani3Weiqian Huan4Zexin Zhao5Yonghua Wang6School of Food Science and Engineering, South China University of Technology, Guangzhou, ChinaSchool of Chemistry and Chemical Engineering, Henan University of Technology, Zhengzhou, ChinaSchool of Food Science and Engineering, South China University of Technology, Guangzhou, ChinaSchool of Bioscience and Bioengineering, South China University of Technology, Guangzhou, ChinaSchool of Bioscience and Bioengineering, South China University of Technology, Guangzhou, ChinaSchool of Bioscience and Bioengineering, South China University of Technology, Guangzhou, ChinaSchool of Food Science and Engineering, South China University of Technology, Guangzhou, ChinaLipases 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.http://journal.frontiersin.org/article/10.3389/fbioe.2017.00016/fulllipaselid domainthermostabilityinterfacial activationprotein engineering |
| spellingShingle | Faez Iqbal Khan Faez Iqbal Khan Dongming Lan Rabia Durrani Weiqian Huan Zexin Zhao Yonghua Wang The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties Frontiers in Bioengineering and Biotechnology lipase lid domain thermostability interfacial activation protein engineering |
| title | The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties |
| title_full | The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties |
| title_fullStr | The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties |
| title_full_unstemmed | The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties |
| title_short | The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties |
| title_sort | lid domain in lipases structural and functional determinant of enzymatic properties |
| topic | lipase lid domain thermostability interfacial activation protein engineering |
| url | http://journal.frontiersin.org/article/10.3389/fbioe.2017.00016/full |
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