Ontology highlight
ABSTRACT:
SUBMITTER: Li Z
PROVIDER: S-EPMC5354503 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Li Zhu Z Kitanishi Kenichi K Twahir Umar T UT Cracan Valentin V Chapman Derrell D Warncke Kurt K Banerjee Ruma R
The Journal of biological chemistry 20170127 10
IcmF is a 5'-deoxyadenosylcobalamin (AdoCbl)-dependent enzyme that catalyzes the carbon skeleton rearrangement of isobutyryl-CoA to butyryl-CoA. It is a bifunctional protein resulting from the fusion of a G-protein chaperone with GTPase activity and the cofactor- and substrate-binding mutase domains with isomerase activity. IcmF is prone to inactivation during catalytic turnover, thus setting up its dependence on a cofactor repair system. Herein, we demonstrate that the GTPase activity of IcmF p ...[more]