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The mycobacterial guaB1 gene encodes a guanosine 5 '-monophosphate reductase with a cystathionine-beta-synthase domain

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00556977" target="_blank" >RIV/61388963:_____/22:00556977 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1111/febs.16448" target="_blank" >https://doi.org/10.1111/febs.16448</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1111/febs.16448" target="_blank" >10.1111/febs.16448</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The mycobacterial guaB1 gene encodes a guanosine 5 '-monophosphate reductase with a cystathionine-beta-synthase domain

  • Original language description

    Mycobacteria express enzymes from both the de novo and purine-salvage pathways. However, the regulation of these processes and the roles of individual metabolic enzymes have not been sufficiently detailed. Both Mycobacterium tuberculosis (Mtb) and Mycobacterium smegmatis (Msm) possess three guaB genes, but information is only available on guaB2, which encodes an essential inosine 5'-monophosphate dehydrogenase (IMPDH) involved in de novo purine biosynthesis. This study shows that guaB1, annotated in databases as a putative IMPDH, encodes a guanosine 5'-monophosphate reductase (GMPR), which recycles guanosine monophosphate to inosine monophosphate within the purine-salvage pathway and contains a cystathionine-beta-synthase domain (CBS), which is essential for enzyme activity. GMPR activity is allosterically regulated by the ATP/GTP ratio in a pH-dependent manner. Bioinformatic analysis has indicated the presence of GMPRs containing CBS domains across the entire Actinobacteria phylum.

  • 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

    <a href="/en/project/EF16_019%2F0000729" target="_blank" >EF16_019/0000729: Chemical biology for drugging undruggable targets</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    FEBS Journal

  • ISSN

    1742-464X

  • e-ISSN

    1742-4658

  • Volume of the periodical

    289

  • Issue of the periodical within the volume

    18

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    28

  • Pages from-to

    5571-5598

  • UT code for WoS article

    000778625500001

  • EID of the result in the Scopus database

    2-s2.0-85127597203