Single time-point analysis of product and substrate inhibition

When enzyme inhibition by either the product or excess substrate occurs, it is possible to determine the characteristic kinetic parameters based on [P]/t measurements, even when a large proportion of the substrate is converted. The advantages of various approaches are discussed. Most of them allow a good estimation of the V and K<sub>m</sub> values. Conversely, the determination of K<sub>p</sub> (product inhibition) and K<sub>i</sub> (inhibition by excess substrate) can be more challenging. In the first case, determination of the type of inhibition requires more complex experiments that are beyond the scope of the present contribution. In the second, the inhibition constant K<sub>i</sub> can only be roughly estimated. In an experimental approach, we compared the results obtained either with initial rate measurements or with 50 to 60% conversion of the substrate. Similar values of V and K<sub>m</sub> were obtained. Measurements involving the conversion of a large proportion of substrate are particularly advantageous when the assay method is difficult or time-consuming, or when obtaining the substrate presents experimental difficulties or involves substantial costs.

Authors

Institutions

Publication Details

Journal
Scientific Reports
Published
2024-10-05
DOI
https://doi.org/10.1038/s41598-024-70805-9
Citations
1
Primary Topic
Mass Spectrometry Techniques and Applications
Type
article
Field-Weighted Citation Impact
0.24
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Single time-point analysis of product and substrate inhibition

Romain Malempré, Wim Versées, Olivier Verlaine, André Matagne et al.
1 citations
Scientific Reports
Mass Spectrometry Techniques and Applications
0.24
article

Single time-point analysis of product and substrate inhibition

Romain Malempré, Wim Versées, Olivier Verlaine, André Matagne, Jean‐Marie Frère
article en
1 citations

Abstract

When enzyme inhibition by either the product or excess substrate occurs, it is possible to determine the characteristic kinetic parameters based on [P]/t measurements, even when a large proportion of the substrate is converted. The advantages of various approaches are discussed. Most of them allow a good estimation of the V and K<sub>m</sub> values. Conversely, the determination of K<sub>p</sub> (product inhibition) and K<sub>i</sub> (inhibition by excess substrate) can be more challenging. In the first case, determination of the type of inhibition requires more complex experiments that are beyond the scope of the present contribution. In the second, the inhibition constant K<sub>i</sub> can only be roughly estimated. In an experimental approach, we compared the results obtained either with initial rate measurements or with 50 to 60% conversion of the substrate. Similar values of V and K<sub>m</sub> were obtained. Measurements involving the conversion of a large proportion of substrate are particularly advantageous when the assay method is difficult or time-consuming, or when obtaining the substrate presents experimental difficulties or involves substantial costs.

Scientific ReportsVol. 14(1)
Vrije Universiteit Brussel (BE), University of Liège (BE), VIB-VUB Center for Structural Biology (BE)
Zero hunger
Openalex Percentile: Top 49%
Mass Spectrometry Techniques and Applications
0.24
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.