Promiscuous Dehalogenase Activity of the Epoxide Hydrolase
CorEH from Corynebacterium sp. C12

J 2021

Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12

SCHUITEN, Eva D., Christoffel P. S. BADENHORST, Gottfried J. PALM, Leona BERNDT, Michael LAMMERS et. al.

Basic information

Original name

Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12

Authors

SCHUITEN, Eva D. (276 Germany), Christoffel P. S. BADENHORST (276 Germany), Gottfried J. PALM (276 Germany), Leona BERNDT (276 Germany), Michael LAMMERS (276 Germany), Jan MIČAN (203 Czech Republic, belonging to the institution), David BEDNÁŘ (203 Czech Republic, belonging to the institution), Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution) and Uwe T. BORNSCHEUER (276 Germany)

Edition

ACS Catalysis, WASHINGTON, AMER CHEMICAL SOC, 2021, 2155-5435

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10403 Physical chemistry

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 13.700

RIV identification code

RIV/00216224:14310/21:00121799

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.1021/acscatal.1c00851

UT WoS

000656056200020

Keywords in English

catalytic promiscuity; Corynebacterium; epoxide hydrolase; haloalkane dehalogenase; dual activity

Abstract

V originále

Haloalkane dehalogenases and epoxide hydrolases are phylogenetically related and structurally homologous enzymes that use nucleophilic aspartate residues for an S(N)2 attack on their substrates. Despite their mechanistic similarities, no enzymes are known that exhibit both epoxide hydrolase and dehalogenase activity. We screened a subset of epoxide hydrolases, closely related to dehalogenases, for dehalogenase activity and found that the epoxide hydrolase CorEH from Corynebacterium sp. C12 exhibits promiscuous dehalogenase activity. Compared to the hydrolysis of epoxides like cyclohexene oxide (1.41 mu mol min(-1) mg(-1)), the dehalogenation of haloalkanes like 1-bromobutane (0.25 nmol min(-1) mg(-1)) is about 5000-fold lower. In addition to the activity with 1-bromobutane, dehalogenase activity was detected with other substrates like 1-bromohexane, 1,2-dibromoethane, 1-iodobutane, and 1-iodohexane. This study shows that dual epoxide hydrolase and dehalogenase activity can be present in one naturally occurring protein scaffold.

Citovat

SCHUITEN, Eva D., Christoffel P. S. BADENHORST, Gottfried J. PALM, Leona BERNDT, Michael LAMMERS, Jan MIČAN, David BEDNÁŘ, Jiří DAMBORSKÝ and Uwe T. BORNSCHEUER. Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12. ACS Catalysis. WASHINGTON: AMER CHEMICAL SOC, 2021, vol. 11, No 10, p. 6113-6120. ISSN 2155-5435. Available from: https://dx.doi.org/10.1021/acscatal.1c00851.

@article{1776763,
   author = {Schuiten, Eva D. and Badenhorst, Christoffel P. S. and Palm, Gottfried J. and Berndt, Leona and Lammers, Michael and Mičan, Jan and Bednář, David and Damborský, Jiří and Bornscheuer, Uwe T.},
   article_location = {WASHINGTON},
   article_number = {10},
   doi = {http://dx.doi.org/10.1021/acscatal.1c00851},
   keywords = {catalytic promiscuity; Corynebacterium; epoxide hydrolase; haloalkane dehalogenase; dual activity},
   language = {eng},
   issn = {2155-5435},
   journal = {ACS Catalysis},
   title = {Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12},
   url = {https://pubs.acs.org/doi/10.1021/acscatal.1c00851},
   volume = {11},
   year = {2021}
}

TY  - JOUR
ID  - 1776763
AU  - Schuiten, Eva D. - Badenhorst, Christoffel P. S. - Palm, Gottfried J. - Berndt, Leona - Lammers, Michael - Mičan, Jan - Bednář, David - Damborský, Jiří - Bornscheuer, Uwe T.
PY  - 2021
TI  - Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12
JF  - ACS Catalysis
VL  - 11
IS  - 10
SP  - 6113-6120
EP  - 6113-6120
PB  - AMER CHEMICAL SOC
SN  - 21555435
KW  - catalytic promiscuity
KW  - Corynebacterium
KW  - epoxide hydrolase
KW  - haloalkane dehalogenase
KW  - dual activity
UR  - https://pubs.acs.org/doi/10.1021/acscatal.1c00851
N2  - Haloalkane dehalogenases and epoxide hydrolases are phylogenetically related and structurally homologous enzymes that use nucleophilic aspartate residues for an S(N)2 attack on their substrates. Despite their mechanistic similarities, no enzymes are known that exhibit both epoxide hydrolase and dehalogenase activity. We screened a subset of epoxide hydrolases, closely related to dehalogenases, for dehalogenase activity and found that the epoxide hydrolase CorEH from Corynebacterium sp. C12 exhibits promiscuous dehalogenase activity. Compared to the hydrolysis of epoxides like cyclohexene oxide (1.41 mu mol min(-1) mg(-1)), the dehalogenation of haloalkanes like 1-bromobutane (0.25 nmol min(-1) mg(-1)) is about 5000-fold lower. In addition to the activity with 1-bromobutane, dehalogenase activity was detected with other substrates like 1-bromohexane, 1,2-dibromoethane, 1-iodobutane, and 1-iodohexane. This study shows that dual epoxide hydrolase and dehalogenase activity can be present in one naturally occurring protein scaffold.
ER  -

SCHUITEN, Eva D., Christoffel P. S. BADENHORST, Gottfried J. PALM, Leona BERNDT, Michael LAMMERS, Jan MIČAN, David BEDNÁŘ, Jiří DAMBORSKÝ and Uwe T. BORNSCHEUER. Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12. \textit{ACS Catalysis}. WASHINGTON: AMER CHEMICAL SOC, 2021, vol.~11, No~10, p.~6113-6120. ISSN~2155-5435. Available from: https://dx.doi.org/10.1021/acscatal.1c00851.

Detailed Information on Publication Record