Structural highlights
Function
[A0A100XBM0_MYCTH] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.[HAMAP-Rule:MF_01964]
Publication Abstract from PubMed
Inosine-5'-monophosphate dehydrogenase (IMPDH) is a rate-limiting enzyme involved in nucleotide biosynthesis. Because of its critical role in purine biosynthesis, IMPDH is a drug design target for immunosuppressive, anticancer, antiviral and antimicrobial chemotherapy. In this study, we use mass spectrometry and X-ray crystallography to show that the inhibitor 6-Cl-purine ribotide forms a covalent adduct with the Cys-341 residue of Mycobacterium thermoresistibile IMPDH.
Covalent inactivation of Mycobacterium thermoresistibile inosine-5'-monophosphate dehydrogenase (IMPDH).,Trapero A, Pacitto A, Chan DS, Abell C, Blundell TL, Ascher DB, Coyne AG Bioorg Med Chem Lett. 2020 Jan 15;30(2):126792. doi: 10.1016/j.bmcl.2019.126792. , Epub 2019 Nov 9. PMID:31757668[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Trapero A, Pacitto A, Chan DS, Abell C, Blundell TL, Ascher DB, Coyne AG. Covalent inactivation of Mycobacterium thermoresistibile inosine-5'-monophosphate dehydrogenase (IMPDH). Bioorg Med Chem Lett. 2020 Jan 15;30(2):126792. doi: 10.1016/j.bmcl.2019.126792. , Epub 2019 Nov 9. PMID:31757668 doi:http://dx.doi.org/10.1016/j.bmcl.2019.126792
