Ontology highlight
ABSTRACT:
SUBMITTER: Smith NE
PROVIDER: S-EPMC3283820 | biostudies-literature | 2012 Feb
REPOSITORIES: biostudies-literature
Biophysical journal 20120221 4
It has been hypothesized that the bifunctional enzyme DmpFG channels its intermediate, acetaldehyde, from one active site to the next using a buried intermolecular channel identified in the crystal structure. This channel appears to switch between an open and a closed conformation depending on whether the coenzyme NAD(+) is present or absent. Here, we applied molecular dynamics and metadynamics to investigate channeling within DmpFG in both the presence and absence of NAD(+). We found that subst ...[more]