Correlation Engine 2.0
Clear Search sequence regions


Sizes of these terms reflect their relevance to your search.

The mechanism of lipase binding to the lipid-water interface is crucial for substrate specificity and kinetic properties. In this study, the chain-length specificity, regiospecificity and substrate specificity of Phospholipase A1 (PLA1) and its parent enzyme Thermomyces lanuginosus lipase (TLL) have been investigated using a classical emulsion system. The results show that both PLA1 and TLL are 1,3-regioselective lipases. Additionally, the hydrolytic activity of PLA1 is comparatively lower on short-chain triacylglyceride (TAG) and higher on phosphatidylcholine (PC) than the hydrolytic activity of TLL. Further, the results obtained with monolayer film techniques demonstrate that the C-terminal region regulates the binding of PLA1 to PC. A hypothesis is presented according to which the α9 helix of C-terminal region in PLA1 not only controls the opening of lid but also serves as a membrane anchor that assists in binding to PC. These findings bring new insight into rational design of novel lipases with intriguing functionalities. Copyright © 2016 Elsevier Inc. All rights reserved.

Citation

Ruipu Xin, Faez Iqbal Khan, Zexin Zhao, Zedong Zhang, Bo Yang, Yonghua Wang. A comparative study on kinetics and substrate specificities of Phospholipase A1 with Thermomyces lanuginosus lipase. Journal of colloid and interface science. 2017 Feb 15;488:149-154

Expand section icon Mesh Tags

Expand section icon Substances


PMID: 27821336

View Full Text