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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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
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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