The use of matrix-assisted laser desorption/ionization mass spectrometry in enzyme activity assays and its position in the context of other available methods
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F23%3A73614691" target="_blank" >RIV/61989592:15310/23:73614691 - isvavai.cz</a>
Result on the web
<a href="https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/epdf/10.1002/mas.21733" target="_blank" >https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/epdf/10.1002/mas.21733</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/mas.21733" target="_blank" >10.1002/mas.21733</a>
Alternative languages
Result language
angličtina
Original language name
The use of matrix-assisted laser desorption/ionization mass spectrometry in enzyme activity assays and its position in the context of other available methods
Original language description
Activity assays are indispensable for studying biochemical properties of enzymes. The purposes of measuring activity are wide ranging from a simple detection of the presence of an enzyme to kinetic experiments evaluating the substrate specificity, reaction mechanisms, and susceptibility to inhibitors. Common activity assay methods include spectroscopy, electrochemical sensors, or liquid chromatography coupled with various detection techniques. This review focuses on the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) as a growing and modern alternative, which offers high speed of analysis, sensitivity, versatility, possibility of automation, and cost-effectiveness. It may reveal reaction intermediates, side products or measure more enzymes at once. The addition of an internal standard or calculating the ratios of the substrate and product peak intensities and areas overcome the inherent inhomogeneous distribution of analyte and matrix in the sample spot, which otherwise results in a poor reproducibility. Examples of the application of MALDI-TOF MS for assaying hydrolases (including peptidases and beta-lactamases for antibiotic resistance tests) and other enzymes are provided. Concluding remarks summarize advantages and challenges coming from the present experience, and draw future perspectives such as a screening of large libraries of chemical compounds for their substrate or inhibitory properties towards enzymes.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10609 - Biochemical research methods
Result continuities
Project
<a href="/en/project/EF16_019%2F0000827" target="_blank" >EF16_019/0000827: Plants as a tool for sustainable global development</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Mass Spectrometry Reviews
ISSN
0277-7037
e-ISSN
1098-2787
Volume of the periodical
42
Issue of the periodical within the volume
3
Country of publishing house
US - UNITED STATES
Number of pages
24
Pages from-to
1008-1031
UT code for WoS article
000697612100001
EID of the result in the Scopus database
2-s2.0-85115248795