The Bateman domain of IMP dehydrogenase is a binding target for dinucleoside polyphosphates.

ABSTRACT: IMP dehydrogenase (IMPDH) is an essential enzyme that catalyzes the rate-limiting step in the de novo guanine nucleotide biosynthetic pathway. Because of its involvement in the control of cell division and proliferation, IMPDH represents a therapeutic for managing several diseases, including microbial infections and cancer. IMPDH must be tightly regulated, but the molecular mechanisms responsible for its physiological regulation remain unknown. To this end, we recently reported an important role of adenine and guanine mononucleotides that bind to the regulatory Bateman domain to allosterically modulate the catalytic activity of eukaryotic IMPDHs. Here, we have used enzyme kinetics, X-ray crystallography, and small-angle X-ray scattering (SAXS) methodologies to demonstrate that adeni

SUBMITTER: Fernandez-Justel D 

PROVIDER: S-EPMC6779442 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature