Dynamic disorder and stepwise deactivation in a chymotrypsin catalyzed hydrolysis reaction

Gert De Cremer; Maarten B.J. Roeffaers; Mukulesh Baruah; Michel Sliwa; Bert F. Sels; Johan Hofkens; Dirk E. De Vos

doi:10.1021/ja077621d

Dynamic disorder and stepwise deactivation in a chymotrypsin catalyzed hydrolysis reaction

Gert De Cremer
, Maarten B.J. Roeffaers
, Mukulesh Baruah
, Michel Sliwa
, Bert F. Sels
, Johan Hofkens
, Dirk E. De Vos

Department of Microbial and Molecular Systems
KU Leuven
Department of Chemistry

Research output: Contribution to journal › Article › peer-review

59 Citations (Scopus)

Abstract

In situ observation of the catalytic activity of individual α-chymotrypsin enzymes reveals a novel pathway for spontaneous deactivation. Rather than deactivating abruptly in a one-step process, the enzyme seems to struggle for life; the activity decreases stepwise with intermittent inactive periods before deactivating irreversibly. During the active periods, dynamic disorder and memory effects are observed, originating from conformational fluctuations within the enzyme's structure.

Original language	English
Pages (from-to)	15458-15459
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	129
Issue number	50
DOIs	https://doi.org/10.1021/ja077621d
Publication status	Published - 19 Dec 2007
Externally published	Yes

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10.1021/ja077621d

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title = "Dynamic disorder and stepwise deactivation in a chymotrypsin catalyzed hydrolysis reaction",

abstract = "In situ observation of the catalytic activity of individual α-chymotrypsin enzymes reveals a novel pathway for spontaneous deactivation. Rather than deactivating abruptly in a one-step process, the enzyme seems to struggle for life; the activity decreases stepwise with intermittent inactive periods before deactivating irreversibly. During the active periods, dynamic disorder and memory effects are observed, originating from conformational fluctuations within the enzyme's structure.",

author = "\{De Cremer\}, Gert and Roeffaers, \{Maarten B.J.\} and Mukulesh Baruah and Michel Sliwa and Sels, \{Bert F.\} and Johan Hofkens and \{De Vos\}, \{Dirk E.\}",

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T1 - Dynamic disorder and stepwise deactivation in a chymotrypsin catalyzed hydrolysis reaction

AU - De Cremer, Gert

AU - Roeffaers, Maarten B.J.

AU - Baruah, Mukulesh

AU - Sliwa, Michel

AU - Sels, Bert F.

AU - Hofkens, Johan

AU - De Vos, Dirk E.

PY - 2007/12/19

Y1 - 2007/12/19

N2 - In situ observation of the catalytic activity of individual α-chymotrypsin enzymes reveals a novel pathway for spontaneous deactivation. Rather than deactivating abruptly in a one-step process, the enzyme seems to struggle for life; the activity decreases stepwise with intermittent inactive periods before deactivating irreversibly. During the active periods, dynamic disorder and memory effects are observed, originating from conformational fluctuations within the enzyme's structure.

AB - In situ observation of the catalytic activity of individual α-chymotrypsin enzymes reveals a novel pathway for spontaneous deactivation. Rather than deactivating abruptly in a one-step process, the enzyme seems to struggle for life; the activity decreases stepwise with intermittent inactive periods before deactivating irreversibly. During the active periods, dynamic disorder and memory effects are observed, originating from conformational fluctuations within the enzyme's structure.

U2 - 10.1021/ja077621d

DO - 10.1021/ja077621d

M3 - Article

C2 - 18031046

AN - SCOPUS:37849031538

SN - 0002-7863

VL - 129

SP - 15458

EP - 15459

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 50

ER -

Dynamic disorder and stepwise deactivation in a chymotrypsin catalyzed hydrolysis reaction

Abstract

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