5x20

Publication Abstract from PubMed

Enterococcus faecium NAD-dependent d-mandelate dehydrogenase (d-ManDH) belongs to a ketopantoate reductase (KPR)-related d-2-hydroxyacid dehydrogenase family, and exhibits broad substrate specificity toward bulky hydrophobic 2-ketoacids, preferring C3-branched substrates. The ternary complex structure of d-ManDH with NADH and anilino(oxo)acetate (AOA) revealed that the substrate binding induces a shear motion of the N-terminal domain along the C-terminal domain, following the hinge motion induced by the NADH binding, and allows the bound NADH molecule to form favorable interactions with a 2-ketoacid substrate. d-ManDH possesses a sufficiently wide pocket that accommodates the C3 branched side chains of substrates like KPR, but unlike the pocket of KPR, the pocket of d-ManDH comprises an entirely hydrophobic surface and an expanded space, in which the AOA benzene is accommodated. The expanded space mostly comprises a mobile loop structure, which likely modulates the shape and size of the space depending on the substrate.

The ternary complex structure of d-mandelate dehydrogenase with NADH and anilino(oxo)acetate.,Furukawa N, Miyanaga A, Nakajima M, Taguchi H Biochem Biophys Res Commun. 2017 Mar 19. pii: S0006-291X(17)30552-1. doi:, 10.1016/j.bbrc.2017.03.088. PMID:28327357^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.