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Cleavage Product Accumulation Decreases the Activity of Cutinase during PET Hydrolysis.

Groß, Christine and Hamacher, Kay and Schmitz, Katja and Jager, Sven :
Cleavage Product Accumulation Decreases the Activity of Cutinase during PET Hydrolysis.
In: Journal of chemical information and modeling, 57 (2) pp. 243-255. ISSN 1549-960X
[Article] , (2017)

Abstract

The Fusarium solani cutinase (FsC) is a promising candidate for the enzymatic degradation of the synthetic polyester polyethylene terephthalate (PET) but still suffers from a lack of activity. Using atomic MD simulations with different concentrations of cleavage product ethylene glycol (EG), we show influences of EG on the dynamic of FsC. We observed accumulation of EG in the active site region reducing the local flexibility of FsC. Furthermore, we used a coarse-grained mechanical model to investigate whether substrate binding in the active site causes an induced fit. We observed this supposed induced fit or "breath-like" movement during substrate binding indicating that the active site has to be flexible for substrate conversion. This guides rational design: mutants with an increased flexibility near the active site should be considered to compensate the solvent-mediated reduction in activity.

Item Type: Article
Erschienen: 2017
Creators: Groß, Christine and Hamacher, Kay and Schmitz, Katja and Jager, Sven
Title: Cleavage Product Accumulation Decreases the Activity of Cutinase during PET Hydrolysis.
Language: English
Abstract:

The Fusarium solani cutinase (FsC) is a promising candidate for the enzymatic degradation of the synthetic polyester polyethylene terephthalate (PET) but still suffers from a lack of activity. Using atomic MD simulations with different concentrations of cleavage product ethylene glycol (EG), we show influences of EG on the dynamic of FsC. We observed accumulation of EG in the active site region reducing the local flexibility of FsC. Furthermore, we used a coarse-grained mechanical model to investigate whether substrate binding in the active site causes an induced fit. We observed this supposed induced fit or "breath-like" movement during substrate binding indicating that the active site has to be flexible for substrate conversion. This guides rational design: mutants with an increased flexibility near the active site should be considered to compensate the solvent-mediated reduction in activity.

Journal or Publication Title: Journal of chemical information and modeling
Volume: 57
Number: 2
Divisions: 10 Department of Biology
10 Department of Biology > Computational Biology and Simulation
Date Deposited: 13 Feb 2017 11:36
Identification Number: pmid:28128951
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