Probing the enantioselectivity of Bacillus subtilis esterase BS2 for tert. alcohols

M Wiggers; J Holt; R Kourist; S Bartsch; Iwce Arends; A J Minnaard; U T Bornscheuer; U Hanefeld

doi:10.1016/j.molcatb.2009.04.003

Probing the enantioselectivity of Bacillus subtilis esterase BS2 for tert. alcohols

M Wiggers, J Holt, R Kourist, S Bartsch, Iwce Arends, A J Minnaard, U T Bornscheuer, U Hanefeld

Institut für Molekulare Biotechnologie (6550)

Publikation: Beitrag in einer Fachzeitschrift › Artikel › Begutachtung

Abstract

The activity and enantioselectivity of several mutants of the esterase BS2 from Bacillus subtilis have been investigated. In the enzymatic hydrolysis of alpha,alpha-disubstituted cyanohydrin acetates, a class of tert. alcohol esters, they were active but not selective. In contrast to this result similar tert. acetylenic alcohol esters were hydrolysed with high E-values (>100). The difference in reactivity has been studied by molecular dynamics studies. The computer model suggested that the source of the observed difference in reactivity between the two very similar tert. alcohol esters lies in the ability of the cyanohydrins to form hydrogen bonds to water molecules-even when the substrate is in the active site. (C) 2009 Elsevier B.V. All rights reserved.

Originalsprache	englisch
Seiten (von - bis)	82-86
Seitenumfang	5
Fachzeitschrift	Journal of Molecular Catalysis B
Jahrgang	60
DOIs	https://doi.org/10.1016/j.molcatb.2009.04.003
Publikationsstatus	Veröffentlicht - 2009

Zugriff auf Dokument

10.1016/j.molcatb.2009.04.003

Dieses zitieren

@article{6e88740c72594061bd808f8546df6d74,

title = "Probing the enantioselectivity of Bacillus subtilis esterase BS2 for tert. alcohols",

abstract = "The activity and enantioselectivity of several mutants of the esterase BS2 from Bacillus subtilis have been investigated. In the enzymatic hydrolysis of alpha,alpha-disubstituted cyanohydrin acetates, a class of tert. alcohol esters, they were active but not selective. In contrast to this result similar tert. acetylenic alcohol esters were hydrolysed with high E-values (>100). The difference in reactivity has been studied by molecular dynamics studies. The computer model suggested that the source of the observed difference in reactivity between the two very similar tert. alcohol esters lies in the ability of the cyanohydrins to form hydrogen bonds to water molecules-even when the substrate is in the active site. (C) 2009 Elsevier B.V. All rights reserved.",

keywords = "Acetylenic alcohol Bacillus subtilis esterase BS2 candida-cylindracea Cyanohydrin cyanohydrin acetates enzyme Enzyme catalysis kinetic resolution lipase mutants tert. alcohol tertiary alcohols",

author = "M Wiggers and J Holt and R Kourist and S Bartsch and Iwce Arends and Minnaard, {A J} and Bornscheuer, {U T} and U Hanefeld",

note = "ISI Document Delivery No.: 461EZ Times Cited: 3 Cited Reference Count: 24 Wiggers, Michiel Holt, Jarle Kourist, Robert Bartsch, Sebastian Arends, Isabel W. C. E. Minnaard, Adriaan J. Bornscheuer, Uwe T. Hanefeld, Ulf Nrsc-c Financial support from the NRSC-C for J.H. is gratefully acknowledged. Elsevier science bv Amsterdam",

year = "2009",

doi = "10.1016/j.molcatb.2009.04.003",

language = "English",

volume = "60",

pages = "82--86",

journal = "Journal of Molecular Catalysis B",

issn = "1381-1177",

publisher = "Elsevier B.V.",

}

TY - JOUR

T1 - Probing the enantioselectivity of Bacillus subtilis esterase BS2 for tert. alcohols

AU - Wiggers, M

AU - Holt, J

AU - Kourist, R

AU - Bartsch, S

AU - Arends, Iwce

AU - Minnaard, A J

AU - Bornscheuer, U T

AU - Hanefeld, U

N1 - ISI Document Delivery No.: 461EZ Times Cited: 3 Cited Reference Count: 24 Wiggers, Michiel Holt, Jarle Kourist, Robert Bartsch, Sebastian Arends, Isabel W. C. E. Minnaard, Adriaan J. Bornscheuer, Uwe T. Hanefeld, Ulf Nrsc-c Financial support from the NRSC-C for J.H. is gratefully acknowledged. Elsevier science bv Amsterdam

PY - 2009

Y1 - 2009

N2 - The activity and enantioselectivity of several mutants of the esterase BS2 from Bacillus subtilis have been investigated. In the enzymatic hydrolysis of alpha,alpha-disubstituted cyanohydrin acetates, a class of tert. alcohol esters, they were active but not selective. In contrast to this result similar tert. acetylenic alcohol esters were hydrolysed with high E-values (>100). The difference in reactivity has been studied by molecular dynamics studies. The computer model suggested that the source of the observed difference in reactivity between the two very similar tert. alcohol esters lies in the ability of the cyanohydrins to form hydrogen bonds to water molecules-even when the substrate is in the active site. (C) 2009 Elsevier B.V. All rights reserved.

AB - The activity and enantioselectivity of several mutants of the esterase BS2 from Bacillus subtilis have been investigated. In the enzymatic hydrolysis of alpha,alpha-disubstituted cyanohydrin acetates, a class of tert. alcohol esters, they were active but not selective. In contrast to this result similar tert. acetylenic alcohol esters were hydrolysed with high E-values (>100). The difference in reactivity has been studied by molecular dynamics studies. The computer model suggested that the source of the observed difference in reactivity between the two very similar tert. alcohol esters lies in the ability of the cyanohydrins to form hydrogen bonds to water molecules-even when the substrate is in the active site. (C) 2009 Elsevier B.V. All rights reserved.

KW - Acetylenic alcohol Bacillus subtilis esterase BS2 candida-cylindracea Cyanohydrin cyanohydrin acetates enzyme Enzyme catalysis kinetic resolution lipase mutants tert. alcohol tertiary alcohols

U2 - 10.1016/j.molcatb.2009.04.003

DO - 10.1016/j.molcatb.2009.04.003

M3 - Article

SN - 1381-1177

VL - 60

SP - 82

EP - 86

JO - Journal of Molecular Catalysis B

JF - Journal of Molecular Catalysis B

ER -

Probing the enantioselectivity of Bacillus subtilis esterase BS2 for tert. alcohols

Abstract

Zugriff auf Dokument

Fingerprint

Dieses zitieren