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Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase

AutorAparicio, David M.; Pérez-Luque, Rosa ; Carpena, Xavi ; Díaz, Mireia; Ferrer, Joan C. ; Loewen, Peter C.; Fita, Ignacio
Palabras claveMalonyl-CoA: Malonyl-CoA Decarboxylase
Malonic Aciduria
Half-of-the-sites Reactivity
Peroxisomes
Mitochondria
Lipid Metabolism
Acetyl Coenzyme A
Fatty Acid Oxidation
Fecha de publicación26-abr-2013
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJournal of Biological Chemistry 288(17): 11907-11919 (2013)
ResumenDecarboxylation 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 per-oxisomal 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-terminal domain with an acetyltransferase fold (GNAT superfamily). Inter-subunit disulfide bridges, Cys-206-Cys-206 and Cys-243-Cys-243, can link the four subunits of the tetramer, imparting positive cooperativity to the catalytic process. The combination of a half-of-the-sites mechanism within each structural heterodimer and positive cooperativity in the tetramer produces a complex regulatory picture that is further complicated by the multiple intracellular locations of the enzyme. Transport into the peroxisome has been investigated by docking human MCD onto the peroxisomal import protein peroxin 5, which revealed interactions that extend beyond the C-terminal targeting motif. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M112.443846
URIhttp://hdl.handle.net/10261/110044
DOI10.1074/jbc.M112.443846
Identificadoresdoi: 10.1074/jbc.M112.443846
issn: 0021-9258
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