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Oligomeric state of hypoxanthine-guanine phosphoribosyltransferase from Mycobacterium tuberculosis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00475283" target="_blank" >RIV/61388963:_____/17:00475283 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.biochi.2016.12.020" target="_blank" >http://dx.doi.org/10.1016/j.biochi.2016.12.020</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.biochi.2016.12.020" target="_blank" >10.1016/j.biochi.2016.12.020</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Oligomeric state of hypoxanthine-guanine phosphoribosyltransferase from Mycobacterium tuberculosis

  • Original language description

    Sedimentation equilibrium and size-exclusion chromatography experiments on Mycobacterium tuberculosis hypoxanthine-guanine phosphoribosyltransferase (MtHGPRT) have established the existence of this enzyme as a reversibly associating mixture of dimeric and tetrameric species in 0.1 M Tris-HC1-0.012 M MgCl2, pH 7.4. Displacement of the equilibrium position towards the larger oligomer by phosphate signifies the probable existence of MtHGPRT as a tetramer in the biological environment. These data thus add credibility to the relevance of considering enzyme function in the light of a published tetrameric structure deduced from X-ray crystallography. Failure of 5-phospho-alpha-D-ribosyl-1pyrophosphate (PRib-PP) to perturb the dimer tetramer equilibrium position indicates the equivalence and independence of binding for this substrate (the first to bind in an ordered sequential mechanism) to the two oligomers. By virtue of the displacement of the equilibrium position towards dimer that is affected by removing MgCl2 from the Tris-HCl buffer, it can be concluded that divalent metal ions, as well as phosphate, can affect the oligomerization. These characteristics of MtHGPRT in solution are correlated with published crystal structures of four enzyme ligand complexes.

  • 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

    10401 - Organic chemistry

Result continuities

  • Project

    <a href="/en/project/GA16-06049S" target="_blank" >GA16-06049S: Inhibitors of 6-oxopurine phosphoribosyltransferases based on acyclic nucleoside phosphonates: Potential novel antibacterial and antiparasitic agents</a><br>

  • 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

    Biochimie

  • ISSN

    0300-9084

  • e-ISSN

  • Volume of the periodical

    135

  • Issue of the periodical within the volume

    Apr

  • Country of publishing house

    FR - FRANCE

  • Number of pages

    9

  • Pages from-to

    6-14

  • UT code for WoS article

    000397694600002

  • EID of the result in the Scopus database

    2-s2.0-85009097004