Document Report Card
Basic Information
ID: ALA4602619
Journal: Bioorg Med Chem Lett
Title: Covalent inactivation of Mycobacterium thermoresistibile inosine-5'-monophosphate dehydrogenase (IMPDH).
Authors: Trapero A, Pacitto A, Chan DS, Abell C, Blundell TL, Ascher DB, Coyne AG.
Abstract: 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.
CiteXplore: 31757668