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Ancestral Haloalkane Dehalogenases Show Robustness and Unique Substrate Specificity

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F17%3A00067125" target="_blank" >RIV/00159816:_____/17:00067125 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14310/17:00095408

  • Result on the web

    <a href="http://dx.doi.org/10.1002/cbic.201700197" target="_blank" >http://dx.doi.org/10.1002/cbic.201700197</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/cbic.201700197" target="_blank" >10.1002/cbic.201700197</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Ancestral Haloalkane Dehalogenases Show Robustness and Unique Substrate Specificity

  • Original language description

    Ancestral sequence reconstruction (ASR) represents a powerful approach for empirical testing structure-function relationships of diverse proteins. We employed ASR to predict sequences of five ancestral haloalkane dehalogenases (HLDs) from the HLD-II subfamily. Genes encoding the inferred ancestral sequences were synthesized and expressed in Escherichia coli, and the resurrected ancestral enzymes (AncHLD1-5) were experimentally characterized. Strikingly, the ancestral HLDs exhibited significantly enhanced thermodynamic stability compared to extant enzymes (Delta T-m up to 24 degrees C), as well as higher specific activities with preference for short multi-substituted halogenated substrates. Moreover, multivariate statistical analysis revealed a shift in the substrate specificity profiles of AncHLD1 and AncHLD2. This is extremely difficult to achieve by rational protein engineering. The study highlights that ASR is an efficient approach for the development of novel biocatalysts and robust templates for directed evolution.

  • 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

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

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

Others

  • Publication year

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    ChemBioChem

  • ISSN

    1439-4227

  • e-ISSN

  • Volume of the periodical

    18

  • Issue of the periodical within the volume

    14

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    9

  • Pages from-to

    1448-1456

  • UT code for WoS article

    000405726100015

  • EID of the result in the Scopus database