Publication

An Esterase with Superior Activity and Enantioselectivity towards 1,2-O-Isopropylideneglycerol Esters Obtained by Protein Design

Godinho, L. F., Reis, C. R., van Merkerk, R., Poelarends, G. J. & Quax, W. J., Nov-2012, In : Advanced Synthesis & Catalysis. 354, 16, p. 3009-3015 7 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Godinho, L. F., Reis, C. R., van Merkerk, R., Poelarends, G. J., & Quax, W. J. (2012). An Esterase with Superior Activity and Enantioselectivity towards 1,2-O-Isopropylideneglycerol Esters Obtained by Protein Design. Advanced Synthesis & Catalysis, 354(16), 3009-3015. https://doi.org/10.1002/adsc.201200211

Author

Godinho, Luis F. ; Reis, C.R. ; van Merkerk, Ronald ; Poelarends, Gerrit J. ; Quax, Wim J. / An Esterase with Superior Activity and Enantioselectivity towards 1,2-O-Isopropylideneglycerol Esters Obtained by Protein Design. In: Advanced Synthesis & Catalysis. 2012 ; Vol. 354, No. 16. pp. 3009-3015.

Harvard

Godinho, LF, Reis, CR, van Merkerk, R, Poelarends, GJ & Quax, WJ 2012, 'An Esterase with Superior Activity and Enantioselectivity towards 1,2-O-Isopropylideneglycerol Esters Obtained by Protein Design', Advanced Synthesis & Catalysis, vol. 354, no. 16, pp. 3009-3015. https://doi.org/10.1002/adsc.201200211

Standard

An Esterase with Superior Activity and Enantioselectivity towards 1,2-O-Isopropylideneglycerol Esters Obtained by Protein Design. / Godinho, Luis F.; Reis, C.R.; van Merkerk, Ronald; Poelarends, Gerrit J.; Quax, Wim J.

In: Advanced Synthesis & Catalysis, Vol. 354, No. 16, 11.2012, p. 3009-3015.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Godinho LF, Reis CR, van Merkerk R, Poelarends GJ, Quax WJ. An Esterase with Superior Activity and Enantioselectivity towards 1,2-O-Isopropylideneglycerol Esters Obtained by Protein Design. Advanced Synthesis & Catalysis. 2012 Nov;354(16):3009-3015. https://doi.org/10.1002/adsc.201200211


BibTeX

@article{d465fd68749c4dc18ef08c4c5ade1b3d,
title = "An Esterase with Superior Activity and Enantioselectivity towards 1,2-O-Isopropylideneglycerol Esters Obtained by Protein Design",
abstract = "The Escherichia coli esterase YbfF displays high activity towards 1,2-O-isopropylideneglycerol (IPG) butyrate and IPG caprylate, and prefers the R-enantiomer of these substrates, producing the S-enantiomer of the IPG product in excess. To improve the potential of the enzyme for the kinetic resolution of racemic esters of IPG, an enhancement of the activity and enantioselectivity would be highly desirable. Molecular docking of the R-enantiomer of both IPG esters into the active site of YbfF allowed the identification of proximal YbfF active site residues. Four residues (25, 124, 185 and 235) were selected as targets for mutagenesis, in order to enhance YbfF activity and enantioselectivity towards IPG esters. Random mutagenesis at positions 25, 124, 185 and 235 yielded several best YbfF variants with enhanced activity and enantioselectivity towards IPG esters. The best YbfF mutant, W235I, exhibited a 2-fold higher enantioselectivity than wild-type YbfF, with an E=38 for IPG butyrate and an E=77 for IPG caprylate. Molecular docking experiments further support the enhanced enantioselectivity shown experimentally and the structural effects of this amino acid substitution on the active site of YbfF are provided. The engineered W235I mutant is an attractive catalyst for practical applications in the kinetic resolution of IPG esters.",
keywords = "enantioselectivity, Escherichia coli, esterases, kinetic resolution, protein engineering, DIRECTED EVOLUTION, BACILLUS-COAGULANS, MOLECULAR DOCKING, ENZYMES, BIOCATALYSTS, RESOLUTION",
author = "Godinho, {Luis F.} and C.R. Reis and {van Merkerk}, Ronald and Poelarends, {Gerrit J.} and Quax, {Wim J.}",
year = "2012",
month = "11",
doi = "10.1002/adsc.201200211",
language = "English",
volume = "354",
pages = "3009--3015",
journal = "Advanced Synthesis & Catalysis",
issn = "1615-4150",
publisher = "WILEY-V C H VERLAG GMBH",
number = "16",

}

RIS

TY - JOUR

T1 - An Esterase with Superior Activity and Enantioselectivity towards 1,2-O-Isopropylideneglycerol Esters Obtained by Protein Design

AU - Godinho, Luis F.

AU - Reis, C.R.

AU - van Merkerk, Ronald

AU - Poelarends, Gerrit J.

AU - Quax, Wim J.

PY - 2012/11

Y1 - 2012/11

N2 - The Escherichia coli esterase YbfF displays high activity towards 1,2-O-isopropylideneglycerol (IPG) butyrate and IPG caprylate, and prefers the R-enantiomer of these substrates, producing the S-enantiomer of the IPG product in excess. To improve the potential of the enzyme for the kinetic resolution of racemic esters of IPG, an enhancement of the activity and enantioselectivity would be highly desirable. Molecular docking of the R-enantiomer of both IPG esters into the active site of YbfF allowed the identification of proximal YbfF active site residues. Four residues (25, 124, 185 and 235) were selected as targets for mutagenesis, in order to enhance YbfF activity and enantioselectivity towards IPG esters. Random mutagenesis at positions 25, 124, 185 and 235 yielded several best YbfF variants with enhanced activity and enantioselectivity towards IPG esters. The best YbfF mutant, W235I, exhibited a 2-fold higher enantioselectivity than wild-type YbfF, with an E=38 for IPG butyrate and an E=77 for IPG caprylate. Molecular docking experiments further support the enhanced enantioselectivity shown experimentally and the structural effects of this amino acid substitution on the active site of YbfF are provided. The engineered W235I mutant is an attractive catalyst for practical applications in the kinetic resolution of IPG esters.

AB - The Escherichia coli esterase YbfF displays high activity towards 1,2-O-isopropylideneglycerol (IPG) butyrate and IPG caprylate, and prefers the R-enantiomer of these substrates, producing the S-enantiomer of the IPG product in excess. To improve the potential of the enzyme for the kinetic resolution of racemic esters of IPG, an enhancement of the activity and enantioselectivity would be highly desirable. Molecular docking of the R-enantiomer of both IPG esters into the active site of YbfF allowed the identification of proximal YbfF active site residues. Four residues (25, 124, 185 and 235) were selected as targets for mutagenesis, in order to enhance YbfF activity and enantioselectivity towards IPG esters. Random mutagenesis at positions 25, 124, 185 and 235 yielded several best YbfF variants with enhanced activity and enantioselectivity towards IPG esters. The best YbfF mutant, W235I, exhibited a 2-fold higher enantioselectivity than wild-type YbfF, with an E=38 for IPG butyrate and an E=77 for IPG caprylate. Molecular docking experiments further support the enhanced enantioselectivity shown experimentally and the structural effects of this amino acid substitution on the active site of YbfF are provided. The engineered W235I mutant is an attractive catalyst for practical applications in the kinetic resolution of IPG esters.

KW - enantioselectivity

KW - Escherichia coli

KW - esterases

KW - kinetic resolution

KW - protein engineering

KW - DIRECTED EVOLUTION

KW - BACILLUS-COAGULANS

KW - MOLECULAR DOCKING

KW - ENZYMES

KW - BIOCATALYSTS

KW - RESOLUTION

U2 - 10.1002/adsc.201200211

DO - 10.1002/adsc.201200211

M3 - Article

VL - 354

SP - 3009

EP - 3015

JO - Advanced Synthesis & Catalysis

JF - Advanced Synthesis & Catalysis

SN - 1615-4150

IS - 16

ER -

ID: 5716142