Imperial College London

Dr Woscholski

Faculty of Natural SciencesDepartment of Chemistry

Reader in Chemical Biology
 
 
 
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Contact

 

+44 (0)20 7594 5305r.woscholski

 
 
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Location

 

301LMolecular Sciences Research HubWhite City Campus

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Summary

 

Publications

Citation

BibTex format

@article{Yang:2022:10.3390/biom12050632,
author = {Yang, H and Woscholski, R},
doi = {10.3390/biom12050632},
journal = {Biomolecules},
title = {A novel high-throughput assay reveals that the temperature induced increases in transphosphatidylation of phospholipase D are dependent on the alcohol acceptor concentration},
url = {http://dx.doi.org/10.3390/biom12050632},
volume = {12},
year = {2022}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Phospholipase D reacts with alcohols or water, transphosphatidylating or hydrolysing lipids such as phosphatidylcholine, generating phosphatidylalcohols or phosphatidic acid, respectively. The enzyme has been employed in many applications making use of the transphosphatidylation reaction and the enzyme’s tolerance for organic solvents in order to synthesize natural and artificial phospholipids. Yet, its catalytic properties with respect to the transphosphatidylation reaction are not well understood. Here, we introduce a novel high-throughput assay, making use of 96-well plates, that employs Fluorescamine for the detection of transphosphatidylated amino alcohols. This assay allowed to monitor the KM and VMax at different temperatures, revealing that the former will be elevated by the temperature, while the latter is increased by a combination of both temperature and alcohol acceptor concentration being elevated, suggesting that increase in temperature may open up a new binding site for the alcohol acceptor.
AU - Yang,H
AU - Woscholski,R
DO - 10.3390/biom12050632
PY - 2022///
SN - 2218-273X
TI - A novel high-throughput assay reveals that the temperature induced increases in transphosphatidylation of phospholipase D are dependent on the alcohol acceptor concentration
T2 - Biomolecules
UR - http://dx.doi.org/10.3390/biom12050632
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000801293000001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://www.mdpi.com/2218-273X/12/5/632
UR - http://hdl.handle.net/10044/1/98171
VL - 12
ER -