Ontology highlight
ABSTRACT:
SUBMITTER: Beaupre BA
PROVIDER: S-EPMC5522708 | biostudies-literature | 2016 Dec
REPOSITORIES: biostudies-literature
Beaupre Brett A BA Roman Joseph V JV Hoag Matthew R MR Meneely Kathleen M KM Silvaggi Nicholas R NR Lamb Audrey L AL Moran Graham R GR
Archives of biochemistry and biophysics 20161018
Renalase catalyzes the oxidation of isomers of β-NAD(P)H that carry the hydride in the 2 or 6 positions of the nicotinamide base to form β-NAD(P)<sup>+</sup>. This activity is thought to alleviate inhibition of multiple β-NAD(P)-dependent enzymes of primary and secondary metabolism by these isomers. Here we present evidence for a variety of ligand binding phenomena relevant to the function of renalase. We offer evidence of the potential for primary metabolism inhibition with structures of malate ...[more]