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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F21%3A00075222" target="_blank" >RIV/00159816:_____/21:00075222 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/21:00121799

Výsledek na webu

<a href="https://pubs.acs.org/doi/10.1021/acscatal.1c00851" target="_blank" >https://pubs.acs.org/doi/10.1021/acscatal.1c00851</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acscatal.1c00851" target="_blank" >10.1021/acscatal.1c00851</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

10403 - Physical chemistry

Projekt

<a href="/cs/project/EF16_026%2F0008451" target="_blank" >EF16_026/0008451: Inženýrství nových biomateriálů a biofarmak pro diagnózu a léčbu cerebrovaskulárních a neurodegenerativních onemocnění</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ACS Catalysis

ISSN

2155-5435

e-ISSN

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Svazek periodika

11

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

6113-6120

Kód UT WoS článku

000656056200020

EID výsledku v databázi Scopus

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