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.

Základní údaje

Originální název

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

Autoři

SCHUITEN, Eva D. (276 Německo), Christoffel P. S. BADENHORST (276 Německo), Gottfried J. PALM (276 Německo), Leona BERNDT (276 Německo), Michael LAMMERS (276 Německo), Jan MIČAN (203 Česká republika, domácí), David BEDNÁŘ (203 Česká republika, domácí), Jiří DAMBORSKÝ (203 Česká republika, garant, domácí) a Uwe T. BORNSCHEUER (276 Německo)

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10403 Physical chemistry

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 13.700

Kód RIV

RIV/00216224:14310/21:00121799

Organizační jednotka

Přírodovědecká fakulta

DOI

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

UT WoS

000656056200020

Klíčová slova anglicky

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

Štítky

podil, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 21. 2. 2023 14:15, Mgr. Marie Šípková, DiS.

Anotace

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 a Uwe T. BORNSCHEUER. Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12. ACS Catalysis. WASHINGTON: AMER CHEMICAL SOC, 2021, roč. 11, č. 10, s. 6113-6120. ISSN 2155-5435. Dostupné z: 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 a Uwe T. BORNSCHEUER. Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12. \textit{ACS Catalysis}. WASHINGTON: AMER CHEMICAL SOC, 2021, roč.~11, č.~10, s.~6113-6120. ISSN~2155-5435. Dostupné z: https://dx.doi.org/10.1021/acscatal.1c00851.

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