Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries

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Standard

Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries. / Ferrandi, Erica Elisa; Sayer, Christopher ; Isupov, Michail N. ; Annovazzi, Celeste ; Marchesi, Carlotta ; Iacobone, Gianluca ; Peng, Xu; Bonch-Osmolovskaya, Elizaveta ; Wohlgemuth, Roland ; Littlechild, Jennifer A. ; Monti, Daniela .

I: F E B S Journal, Bind 282, Nr. 15, 2015, s. 2879-2894.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Ferrandi, EE, Sayer, C, Isupov, MN, Annovazzi, C, Marchesi, C, Iacobone, G, Peng, X, Bonch-Osmolovskaya, E, Wohlgemuth, R, Littlechild, JA & Monti, D 2015, 'Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries', F E B S Journal, bind 282, nr. 15, s. 2879-2894. https://doi.org/10.1111/febs.13328

APA

Ferrandi, E. E., Sayer, C., Isupov, M. N., Annovazzi, C., Marchesi, C., Iacobone, G., Peng, X., Bonch-Osmolovskaya, E., Wohlgemuth, R., Littlechild, J. A., & Monti, D. (2015). Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries. F E B S Journal, 282(15), 2879-2894. https://doi.org/10.1111/febs.13328

Vancouver

Ferrandi EE, Sayer C, Isupov MN, Annovazzi C, Marchesi C, Iacobone G o.a. Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries. F E B S Journal. 2015;282(15):2879-2894. https://doi.org/10.1111/febs.13328

Author

Ferrandi, Erica Elisa ; Sayer, Christopher ; Isupov, Michail N. ; Annovazzi, Celeste ; Marchesi, Carlotta ; Iacobone, Gianluca ; Peng, Xu ; Bonch-Osmolovskaya, Elizaveta ; Wohlgemuth, Roland ; Littlechild, Jennifer A. ; Monti, Daniela . / Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries. I: F E B S Journal. 2015 ; Bind 282, Nr. 15. s. 2879-2894.

Bibtex

@article{df2a917c52d4408d81b86b6f89912a69,
title = "Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries",
abstract = "The epoxide hydrolases (EHs) represent an attractive option for the synthesis of chiral epoxides and 1,2-diols which are valuable building blocks for the synthesis of several pharmaceutical compounds. A metagenomic approach has been used to identify two new members of the atypical EH limonene-1,2-epoxide hydrolase (LEH) family of enzymes. These two LEHs (Tomsk-LEH and CH55-LEH) show EH activities towards different epoxide substrates, differing in most cases from those previously identified for Rhodococcus erythropolis (Re-LEH) in terms of stereoselectivity. Tomsk-LEH and CH55-LEH, both from thermophilic sources, have higher optimal temperatures and apparent melting temperatures than Re-LEH. The new LEH enzymes have been crystallized and their structures solved to high resolution in the native form and in complex with the inhibitor valpromide for Tomsk-LEH and poly(ethylene glycol) for CH55-LEH. The structural analysis has provided insights into the LEH mechanism, substrate specificity and stereoselectivity of these new LEH enzymes, which has been supported by mutagenesis studies.",
author = "Ferrandi, {Erica Elisa} and Christopher Sayer and Isupov, {Michail N.} and Celeste Annovazzi and Carlotta Marchesi and Gianluca Iacobone and Xu Peng and Elizaveta Bonch-Osmolovskaya and Roland Wohlgemuth and Littlechild, {Jennifer A.} and Daniela Monti",
year = "2015",
doi = "10.1111/febs.13328",
language = "English",
volume = "282",
pages = "2879--2894",
journal = "F E B S Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "15",

}

RIS

TY - JOUR

T1 - Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries

AU - Ferrandi, Erica Elisa

AU - Sayer, Christopher

AU - Isupov, Michail N.

AU - Annovazzi, Celeste

AU - Marchesi, Carlotta

AU - Iacobone, Gianluca

AU - Peng, Xu

AU - Bonch-Osmolovskaya, Elizaveta

AU - Wohlgemuth, Roland

AU - Littlechild, Jennifer A.

AU - Monti, Daniela

PY - 2015

Y1 - 2015

N2 - The epoxide hydrolases (EHs) represent an attractive option for the synthesis of chiral epoxides and 1,2-diols which are valuable building blocks for the synthesis of several pharmaceutical compounds. A metagenomic approach has been used to identify two new members of the atypical EH limonene-1,2-epoxide hydrolase (LEH) family of enzymes. These two LEHs (Tomsk-LEH and CH55-LEH) show EH activities towards different epoxide substrates, differing in most cases from those previously identified for Rhodococcus erythropolis (Re-LEH) in terms of stereoselectivity. Tomsk-LEH and CH55-LEH, both from thermophilic sources, have higher optimal temperatures and apparent melting temperatures than Re-LEH. The new LEH enzymes have been crystallized and their structures solved to high resolution in the native form and in complex with the inhibitor valpromide for Tomsk-LEH and poly(ethylene glycol) for CH55-LEH. The structural analysis has provided insights into the LEH mechanism, substrate specificity and stereoselectivity of these new LEH enzymes, which has been supported by mutagenesis studies.

AB - The epoxide hydrolases (EHs) represent an attractive option for the synthesis of chiral epoxides and 1,2-diols which are valuable building blocks for the synthesis of several pharmaceutical compounds. A metagenomic approach has been used to identify two new members of the atypical EH limonene-1,2-epoxide hydrolase (LEH) family of enzymes. These two LEHs (Tomsk-LEH and CH55-LEH) show EH activities towards different epoxide substrates, differing in most cases from those previously identified for Rhodococcus erythropolis (Re-LEH) in terms of stereoselectivity. Tomsk-LEH and CH55-LEH, both from thermophilic sources, have higher optimal temperatures and apparent melting temperatures than Re-LEH. The new LEH enzymes have been crystallized and their structures solved to high resolution in the native form and in complex with the inhibitor valpromide for Tomsk-LEH and poly(ethylene glycol) for CH55-LEH. The structural analysis has provided insights into the LEH mechanism, substrate specificity and stereoselectivity of these new LEH enzymes, which has been supported by mutagenesis studies.

U2 - 10.1111/febs.13328

DO - 10.1111/febs.13328

M3 - Journal article

C2 - 26032250

VL - 282

SP - 2879

EP - 2894

JO - F E B S Journal

JF - F E B S Journal

SN - 1742-464X

IS - 15

ER -

ID: 152955909