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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

    RIV/00216224:14310/21:00121799

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

Result continuities

  • Project

    <a href="/en/project/EF16_026%2F0008451" target="_blank" >EF16_026/0008451: Engineering of new biomaterials and biopharmaceuticals for the diagnosis and treatment of the cerebrovascular and neurodegenerative diseases</a><br>

  • Continuities

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

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    ACS Catalysis

  • ISSN

    2155-5435

  • e-ISSN

  • Volume of the periodical

    11

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

    6113-6120

  • UT code for WoS article

    000656056200020

  • EID of the result in the Scopus database