Studies on the mechanism of crown-ether-induced activation of enzymes in non-aqueous media

D.J. van Unen; Johannes F.J. Engbersen; David Reinhoudt

doi:10.1016/S1381-1177(00)00033-3

Studies on the mechanism of crown-ether-induced activation of enzymes in non-aqueous media

D.J. van Unen, Johannes F.J. Engbersen, David Reinhoudt

Faculty of Science and Technology

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

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Abstract

Studies on the mechanism of crown-ether-induced activation are described in this paper. Michaelis Menten kinetics of α-chymotrypsin in toluene in the presence and absence of 18-crown-6 showed that only Vmax is increased upon crown ether treatment. Parallel Lineweaver–Burk plots indicate that crown ethers do not activate the enzyme by specific interactions in the active site, such as transition state stabilization or facilitated transport of water molecules. Increased Vmax values of crown-ether-treated enzyme most probably originate from conformational changes, which alter kcat as well as the amount of catalytically active enzyme.

Original language	Undefined
Pages (from-to)	877-882
Journal	Journal of molecular catalysis. B: Enzymatic
Volume	11
Issue number	4-6
DOIs	https://doi.org/10.1016/S1381-1177(00)00033-3
Publication status	Published - 2001

Keywords

METIS-202323
IR-36563

Access to Document

10.1016/S1381-1177(00)00033-3

Cite this

@article{a801fd4ad49f4b7895bea11897513a09,

title = "Studies on the mechanism of crown-ether-induced activation of enzymes in non-aqueous media",

abstract = "Studies on the mechanism of crown-ether-induced activation are described in this paper. Michaelis Menten kinetics of α-chymotrypsin in toluene in the presence and absence of 18-crown-6 showed that only Vmax is increased upon crown ether treatment. Parallel Lineweaver–Burk plots indicate that crown ethers do not activate the enzyme by specific interactions in the active site, such as transition state stabilization or facilitated transport of water molecules. Increased Vmax values of crown-ether-treated enzyme most probably originate from conformational changes, which alter kcat as well as the amount of catalytically active enzyme.",

keywords = "METIS-202323, IR-36563",

author = "{van Unen}, D.J. and Engbersen, {Johannes F.J.} and David Reinhoudt",

note = "α-Chymotrypsin; Crown ethers; Organic solvents ",

year = "2001",

doi = "10.1016/S1381-1177(00)00033-3",

language = "Undefined",

volume = "11",

pages = "877--882",

journal = "Journal of molecular catalysis. B: Enzymatic",

issn = "1381-1177",

publisher = "Elsevier",

number = "4-6",

}

TY - JOUR

T1 - Studies on the mechanism of crown-ether-induced activation of enzymes in non-aqueous media

AU - van Unen, D.J.

AU - Engbersen, Johannes F.J.

AU - Reinhoudt, David

N1 - α-Chymotrypsin; Crown ethers; Organic solvents

PY - 2001

Y1 - 2001

N2 - Studies on the mechanism of crown-ether-induced activation are described in this paper. Michaelis Menten kinetics of α-chymotrypsin in toluene in the presence and absence of 18-crown-6 showed that only Vmax is increased upon crown ether treatment. Parallel Lineweaver–Burk plots indicate that crown ethers do not activate the enzyme by specific interactions in the active site, such as transition state stabilization or facilitated transport of water molecules. Increased Vmax values of crown-ether-treated enzyme most probably originate from conformational changes, which alter kcat as well as the amount of catalytically active enzyme.

AB - Studies on the mechanism of crown-ether-induced activation are described in this paper. Michaelis Menten kinetics of α-chymotrypsin in toluene in the presence and absence of 18-crown-6 showed that only Vmax is increased upon crown ether treatment. Parallel Lineweaver–Burk plots indicate that crown ethers do not activate the enzyme by specific interactions in the active site, such as transition state stabilization or facilitated transport of water molecules. Increased Vmax values of crown-ether-treated enzyme most probably originate from conformational changes, which alter kcat as well as the amount of catalytically active enzyme.

KW - METIS-202323

KW - IR-36563

U2 - 10.1016/S1381-1177(00)00033-3

DO - 10.1016/S1381-1177(00)00033-3

M3 - Article

SN - 1381-1177

VL - 11

SP - 877

EP - 882

JO - Journal of molecular catalysis. B: Enzymatic

JF - Journal of molecular catalysis. B: Enzymatic

IS - 4-6

ER -