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

0556977 - ÚOCHB 2023 RIV GB eng J - Journal Article
Knejzlík, Zdeněk - Doležal, Michal - Herkommerová, Klára - Clarová, Kamila - Klíma, Martin - Dedola, Matteo - Zborníková, Eva - Rejman, Dominik - Pichová, Iva
The mycobacterial guaB1 gene encodes a guanosine 5 '-monophosphate reductase with a cystathionine-beta-synthase domain.
FEBS Journal. Roč. 289, č. 18 (2022), s. 5571-5598. ISSN 1742-464X. E-ISSN 1742-4658
R&D Projects: GA MŠMT(CZ) EF16_019/0000729
Institutional support: RVO:61388963
Keywords : CBS domain * GMPR * guaB1 * Mycobacterium * purine biosynthesis
OECD category: Biochemistry and molecular biology
Impact factor: 5.4, year: 2022
Method of publishing: Open access
https://doi.org/10.1111/febs.16448

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.
Permanent Link: http://hdl.handle.net/11104/0331102


Research data: Worldwide PDB, Worldwide PDB