Dataset Information
Cryo-EM structure of E. coli MaeB acetyl-CoA bound form and the ME domain dimer
Ontology highlight
ABSTRACT:
SUBMITTER: Munetoshi Sassa
PROVIDER: EMPIAR-12692 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Divergent acetyl-CoA binding modes mediate allosteric inhibition of bacterial hybrid-type malic enzymes.
The Journal of biological chemistry 20251104 12
Malic enzymes (MEs) function as the bypass enzyme in the Krebs cycle and have attracted attention in a wide range of scientific and industrial fields. In contrast to eukaryotic MEs, there is currently a lack of understanding of the structure-function relationships of prokaryotic MEs. Especially, little is known about an allosteric inhibition mechanism by an effector ligand in multi-domain MEs called hybrid-type MEs. Many bacterial hybrid-type MEs are inhibited by acetyl-CoA; however, the propose ...[more]
