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Exploration of GH94 Sequence Space for Enzyme Discovery Reveals a Novel Glucosylgalactose Phosphorylase Specificity

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F21%3A00549584" target="_blank" >RIV/61388971:_____/21:00549584 - isvavai.cz</a>

  • Result on the web

    <a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/epdf/10.1002/cbic.202100401" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/epdf/10.1002/cbic.202100401</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/cbic.202100401" target="_blank" >10.1002/cbic.202100401</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Exploration of GH94 Sequence Space for Enzyme Discovery Reveals a Novel Glucosylgalactose Phosphorylase Specificity

  • Original language description

    The substantial increase in DNA sequencing efforts has led to a rapid expansion of available sequences in glycoside hydrolase families. The ever-increasing sequence space presents considerable opportunities for the search for enzymes with novel functionalities. In this work, the sequence-function space of glycoside hydrolase family 94 (GH94) was explored in detail, using a combined approach of phylogenetic analysis and sequence similarity networks. The identification and experimental screening of unknown clusters led to the discovery of an enzyme from the soil bacterium Paenibacillus polymyxa that acts as a 4-O-beta-d-glucosyl-d-galactose phosphorylase (GGalP), a specificity that has not been reported to date. Detailed characterization of GGalP revealed that its kinetic parameters were consistent with those of other known phosphorylases. Furthermore, the enzyme could be used for production of the rare disaccharides 4-O-beta-d-glucosyl-d-galactose and 4-O-beta-d-glucosyl-l-arabinose. Our current work highlights the power of rational sequence space exploration in the search for novel enzyme specificities, as well as the potential of phosphorylases for rare disaccharide synthesis.

  • 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

    2021

  • 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

    1439-7633

  • Volume of the periodical

    22

  • Issue of the periodical within the volume

    23

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    7

  • Pages from-to

    3319-3325

  • UT code for WoS article

    000704237900001

  • EID of the result in the Scopus database

    2-s2.0-85116443660