Single-enzyme kinetics of CALB-catalyzed hydrolysis

Kelly Velonia; Ophir Flomenbom; Davey Loos; Sadahiro Masuo; Mircea Cotlet; Yves Engelborghs; Johan Hofkens; Alan E. Rowan; Joseph Klafter; Roeland J.M. Nolte; Frans C. De Schryver

doi:10.1002/anie.200460625

Single-enzyme kinetics of CALB-catalyzed hydrolysis

Kelly Velonia^*, Ophir Flomenbom, Davey Loos, Sadahiro Masuo, Mircea Cotlet, Yves Engelborghs, Johan Hofkens, Alan E. Rowan, Joseph Klafter, Roeland J.M. Nolte, Frans C. De Schryver

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Abstract

Real-time measurement of the catalysis and substrate kinetics of a single-enzyme hydrolysis reaction is demonstrated with confocal fluorescence microscopy (CFM; see picture, green = CFM beam). A single lipase is shown to have a broad range of conformations; each conformation contributes to the overall enzymatic activity, an observation that is often masked by ensemble measurements.

Original language	English
Pages (from-to)	560-564
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	44
Issue number	4
DOIs	https://doi.org/10.1002/anie.200460625
State	Published - 14 Jan 2005

Keywords

Analytical methods
Enzymes
Fluorescence microscopy
Kinetics
Single-molecule studies

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10.1002/anie.200460625

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title = "Single-enzyme kinetics of CALB-catalyzed hydrolysis",

abstract = "Real-time measurement of the catalysis and substrate kinetics of a single-enzyme hydrolysis reaction is demonstrated with confocal fluorescence microscopy (CFM; see picture, green = CFM beam). A single lipase is shown to have a broad range of conformations; each conformation contributes to the overall enzymatic activity, an observation that is often masked by ensemble measurements.",

keywords = "Analytical methods, Enzymes, Fluorescence microscopy, Kinetics, Single-molecule studies",

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AU - Velonia, Kelly

AU - Flomenbom, Ophir

AU - Loos, Davey

AU - Masuo, Sadahiro

AU - Cotlet, Mircea

AU - Engelborghs, Yves

AU - Hofkens, Johan

AU - Rowan, Alan E.

AU - Klafter, Joseph

AU - Nolte, Roeland J.M.

AU - De Schryver, Frans C.

PY - 2005/1/14

Y1 - 2005/1/14

N2 - Real-time measurement of the catalysis and substrate kinetics of a single-enzyme hydrolysis reaction is demonstrated with confocal fluorescence microscopy (CFM; see picture, green = CFM beam). A single lipase is shown to have a broad range of conformations; each conformation contributes to the overall enzymatic activity, an observation that is often masked by ensemble measurements.

AB - Real-time measurement of the catalysis and substrate kinetics of a single-enzyme hydrolysis reaction is demonstrated with confocal fluorescence microscopy (CFM; see picture, green = CFM beam). A single lipase is shown to have a broad range of conformations; each conformation contributes to the overall enzymatic activity, an observation that is often masked by ensemble measurements.

KW - Analytical methods

KW - Enzymes

KW - Fluorescence microscopy

KW - Kinetics

KW - Single-molecule studies

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 4

ER -

Single-enzyme kinetics of CALB-catalyzed hydrolysis

Abstract

Keywords

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