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240209s2024 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.3c02658
|2 doi
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|a eng
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| 100 |
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|a Hanisch, Daniel T
|e verfasserin
|4 aut
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|a Specific Regulation of Enzymatic Activity by Interface Pulses
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|c 2024
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Revised 08.02.2024
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|a published: Print-Electronic
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|a Citation Status Publisher
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|a The thermodynamic state of the interface in which an enzyme is embedded can regulate the enzymatic activity. Indeed, it has been demonstrated by others and us that close to the maximum in compressibility, the activity of the enzyme is at a maximum as well. Pulses propagating along the interface can modulate the interface state and were demonstrated to be able to modulate the activity of interface-associated acetylcholinesterase (AChE). Here, we demonstrate that enzyme activity modulation by interface pulses depends specifically on the pulse type. Using membrane-embedded enzyme phospholipase A2 (PLA2), enzyme activity can be monitored by detecting the lateral pressure without an additional assay required. We show that pulses that shift the state toward higher pressure and higher lateral density increase the enzymatic activity, while pulses that reduce the pressure induce the opposite effect. These results further support a physical mechanism for enzyme-enzyme communication where compressibility, lateral density, and pressure (thermodynamic state) and not specific molecular modifications regulate enzymatic activity
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|a Journal Article
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|a Schneider, Matthias F
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g (2024) vom: 08. Feb.
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|x 1520-5827
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|g day:08
|g month:02
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|u http://dx.doi.org/10.1021/acs.langmuir.3c02658
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