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
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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
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