7r50 | pdb_00007r50
Crystal structure of GMP reductase from mycobacterium smegmatis in complex with GMP.
Structural highlights
FunctionGUAB1_MYCS2 Involved in the purine-salvage pathway (PubMed:35338694). Catalyzes the NADPH-dependent conversion of GMP to IMP (PubMed:35338694). Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP (PubMed:35338694).[1] Publication Abstract from PubMedMycobacteria 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. The mycobacterial guaB1 gene encodes a guanosine 5'-monophosphate reductase with a cystathionine-beta-synthase domain.,Knejzlik Z, Dolezal M, Herkommerova K, Clarova K, Klima M, Dedola M, Zbornikova E, Rejman D, Pichova I FEBS J. 2022 Mar 26. doi: 10.1111/febs.16448. PMID:35338694[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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