Ontology highlight
ABSTRACT:
SUBMITTER: Aparicio D
PROVIDER: S-EPMC3636878 | biostudies-literature | 2013 Apr
REPOSITORIES: biostudies-literature
Aparicio David D Pérez-Luque Rosa R Carpena Xavier X Díaz Mireia M Ferrer Joan C JC Loewen Peter C PC Fita Ignacio I
The Journal of biological chemistry 20130311 17
Decarboxylation of malonyl-CoA to acetyl-CoA by malonyl-CoA decarboxylase (MCD; EC 4.1.1.9) is an essential facet in the regulation of fatty acid metabolism. The structure of human peroxisomal MCD reveals a molecular tetramer that is best described as a dimer of structural heterodimers, in which the two subunits present markedly different conformations. This molecular organization is consistent with half-of-the-sites reactivity. Each subunit has an all-helix N-terminal domain and a catalytic C-t ...[more]