Enzyme kinetics by real-time quantitative NMR (qNMR) spectroscopy with progress curve analysis
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved..
This review article summarizes how the experimental data obtained using quantitative nuclear magnetic resonance (qNMR) spectroscopy can be combined with progress curve analysis to determine enzyme kinetic parameters. The qNMR approach enables following the enzymatic conversion of the substrate to the product in real-time by a continuous collection of spectra. The Lambert-W function, a closed-form solution to the time-dependent substrate/product kinetics of the rate equation, can estimate the Michaelis-Menten constant (KM.) and the maximum velocity (Vmax) from a single experiment. This article highlights how the qNMR data is well suited for analysis using the Lambert-W function with three different applications. Results from studies on acetylcholinesterase (acetylcholine to acetic acid and choline), β-Galactosidase (lactose to glucose and galactose), and invertase (sucrose to glucose and fructose) are presented. Furthermore, an additional example of how the progress curve analysis is applied to understand the inhibitory role of the artificial sweetener sucralose on sucrose's enzymatic conversion by invertase is discussed. With the wide availability of NMR spectrometers in academia and industries, including bench-top systems with permanent magnets, and the potential to enhance sensitivity using dynamic nuclear polarization in combination with ultrafast methods, the NMR-based enzyme kinetics could be considered a valuable tool for broader applications in the field of enzyme kinetics.
Medienart: |
E-Artikel |
---|
Erscheinungsjahr: |
2022 |
---|---|
Erschienen: |
2022 |
Enthalten in: |
Zur Gesamtaufnahme - volume:658 |
---|---|
Enthalten in: |
Analytical biochemistry - 658(2022) vom: 01. Dez., Seite 114919 |
Sprache: |
Englisch |
---|
Beteiligte Personen: |
Vang, Justin Y [VerfasserIn] |
---|
Links: |
---|
Anmerkungen: |
Date Completed 25.10.2022 Date Revised 30.11.2022 published: Print-Electronic Citation Status MEDLINE |
---|
doi: |
10.1016/j.ab.2022.114919 |
---|
funding: |
|
---|---|
Förderinstitution / Projekttitel: |
|
PPN (Katalog-ID): |
NLM346710952 |
---|
LEADER | 01000naa a22002652 4500 | ||
---|---|---|---|
001 | NLM346710952 | ||
003 | DE-627 | ||
005 | 20231226032115.0 | ||
007 | cr uuu---uuuuu | ||
008 | 231226s2022 xx |||||o 00| ||eng c | ||
024 | 7 | |a 10.1016/j.ab.2022.114919 |2 doi | |
028 | 5 | 2 | |a pubmed24n1155.xml |
035 | |a (DE-627)NLM346710952 | ||
035 | |a (NLM)36154835 | ||
035 | |a (PII)S0003-2697(22)00379-7 | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
041 | |a eng | ||
100 | 1 | |a Vang, Justin Y |e verfasserin |4 aut | |
245 | 1 | 0 | |a Enzyme kinetics by real-time quantitative NMR (qNMR) spectroscopy with progress curve analysis |
264 | 1 | |c 2022 | |
336 | |a Text |b txt |2 rdacontent | ||
337 | |a ƒaComputermedien |b c |2 rdamedia | ||
338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
500 | |a Date Completed 25.10.2022 | ||
500 | |a Date Revised 30.11.2022 | ||
500 | |a published: Print-Electronic | ||
500 | |a Citation Status MEDLINE | ||
520 | |a Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved. | ||
520 | |a This review article summarizes how the experimental data obtained using quantitative nuclear magnetic resonance (qNMR) spectroscopy can be combined with progress curve analysis to determine enzyme kinetic parameters. The qNMR approach enables following the enzymatic conversion of the substrate to the product in real-time by a continuous collection of spectra. The Lambert-W function, a closed-form solution to the time-dependent substrate/product kinetics of the rate equation, can estimate the Michaelis-Menten constant (KM.) and the maximum velocity (Vmax) from a single experiment. This article highlights how the qNMR data is well suited for analysis using the Lambert-W function with three different applications. Results from studies on acetylcholinesterase (acetylcholine to acetic acid and choline), β-Galactosidase (lactose to glucose and galactose), and invertase (sucrose to glucose and fructose) are presented. Furthermore, an additional example of how the progress curve analysis is applied to understand the inhibitory role of the artificial sweetener sucralose on sucrose's enzymatic conversion by invertase is discussed. With the wide availability of NMR spectrometers in academia and industries, including bench-top systems with permanent magnets, and the potential to enhance sensitivity using dynamic nuclear polarization in combination with ultrafast methods, the NMR-based enzyme kinetics could be considered a valuable tool for broader applications in the field of enzyme kinetics | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Review | |
650 | 4 | |a Acetylcholinesterase | |
650 | 4 | |a Enzyme kinetics | |
650 | 4 | |a Invertase | |
650 | 4 | |a Nuclear magnetic resonance (NMR) | |
650 | 4 | |a Progress curve analysis | |
650 | 4 | |a β-Galactosidase | |
650 | 7 | |a beta-Fructofuranosidase |2 NLM | |
650 | 7 | |a EC 3.2.1.26 |2 NLM | |
650 | 7 | |a Acetylcholinesterase |2 NLM | |
650 | 7 | |a EC 3.1.1.7 |2 NLM | |
650 | 7 | |a Lactose |2 NLM | |
650 | 7 | |a J2B2A4N98G |2 NLM | |
650 | 7 | |a Galactose |2 NLM | |
650 | 7 | |a X2RN3Q8DNE |2 NLM | |
650 | 7 | |a Acetylcholine |2 NLM | |
650 | 7 | |a N9YNS0M02X |2 NLM | |
650 | 7 | |a Sucrose |2 NLM | |
650 | 7 | |a 57-50-1 |2 NLM | |
650 | 7 | |a Fructose |2 NLM | |
650 | 7 | |a 30237-26-4 |2 NLM | |
650 | 7 | |a beta-Galactosidase |2 NLM | |
650 | 7 | |a EC 3.2.1.23 |2 NLM | |
650 | 7 | |a Glucose |2 NLM | |
650 | 7 | |a IY9XDZ35W2 |2 NLM | |
650 | 7 | |a Sweetening Agents |2 NLM | |
650 | 7 | |a Choline |2 NLM | |
650 | 7 | |a N91BDP6H0X |2 NLM | |
700 | 1 | |a Breceda, Candido |c Jr |e verfasserin |4 aut | |
700 | 1 | |a Her, Cheenou |e verfasserin |4 aut | |
700 | 1 | |a Krishnan, V V |e verfasserin |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Analytical biochemistry |d 1960 |g 658(2022) vom: 01. Dez., Seite 114919 |w (DE-627)NLM000012556 |x 1096-0309 |7 nnns |
773 | 1 | 8 | |g volume:658 |g year:2022 |g day:01 |g month:12 |g pages:114919 |
856 | 4 | 0 | |u http://dx.doi.org/10.1016/j.ab.2022.114919 |3 Volltext |
912 | |a GBV_USEFLAG_A | ||
912 | |a GBV_NLM | ||
951 | |a AR | ||
952 | |d 658 |j 2022 |b 01 |c 12 |h 114919 |