Removing the Active‐Site Flap in Lipase A from Candida antarctica Produces a Functional Enzyme without Interfacial Activation
Abstract A mobile region is proposed to be a flap that covers the active site of Candida antarctica lipase A. Removal of the mobile region retains the functional properties of the enzyme. Interestingly interfacial activation, required for the wild‐type enzyme, was not observed for the truncated vari...
| Published in: | ChemBioChem |
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| Main Authors: | , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
2015
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1002/cbic.201500471 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcbic.201500471 http://onlinelibrary.wiley.com/wol1/doi/10.1002/cbic.201500471/fullpdf |
| Summary: | Abstract A mobile region is proposed to be a flap that covers the active site of Candida antarctica lipase A. Removal of the mobile region retains the functional properties of the enzyme. Interestingly interfacial activation, required for the wild‐type enzyme, was not observed for the truncated variant, although stability, activity, and stereoselectivity were very similar for the wild‐type and variant enzymes. The variant followed classical Michaelis–Menten kinetics, unlike the wild type. Both gave the same relative specificity in the transacylation of a primary and a secondary alcohol in organic solvent. Furthermore, both showed the same enantioselectivity in transacylation of alcohols and the hydrolysis of alcohol esters, as well as in the hydrolysis of esters chiral at the acid part. |
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