000087594 001__ 87594
000087594 005__ 20230706131403.0
000087594 0247_ $$2doi$$a10.3390/ijms20246124
000087594 0248_ $$2sideral$$a115805
000087594 037__ $$aART-2019-115805
000087594 041__ $$aeng
000087594 100__ $$0(orcid)0000-0001-9962-2157$$aArnedo, María$$uUniversidad de Zaragoza
000087594 245__ $$aMore than one HMG-CoA Lyase: The classical mitochondrial enzyme plus the peroxisomal and the cytosolic ones
000087594 260__ $$c2019
000087594 5060_ $$aAccess copy available to the general public$$fUnrestricted
000087594 5203_ $$aThere are three human enzymes with HMG-CoA lyase activity that are able to synthesize ketone bodies in different subcellular compartments. The mitochondrial HMG-CoA lyase was the first to be described, and catalyzes the cleavage of 3-hydroxy-3-methylglutaryl CoA to acetoacetate and acetyl-CoA, the common final step in ketogenesis and leucine catabolism. This protein is mainly expressed in the liver and its function is metabolic, since it produces ketone bodies as energetic fuels when glucose levels are low. Another isoform is encoded by the same gene for the mitochondrial HMG-CoA lyase (HMGCL), but it is located in peroxisomes. The last HMG-CoA lyase to be described is encoded by a different gene, HMGCLL1, and is located in the cytosolic side of the endoplasmic reticulum membrane. Some activity assays and tissue distribution of this enzyme have shown the brain and lung as key tissues for studying its function. Although the roles of the peroxisomal and cytosolic HMG-CoA lyases remain unknown, recent studies highlight the role of ketone bodies in metabolic remodeling, homeostasis, and signaling, providing new insights into the molecular and cellular function of these enzymes.
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000087594 590__ $$a4.556$$b2019
000087594 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b74 / 296 = 0.25$$c2019$$dQ1$$eT1
000087594 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b48 / 176 = 0.273$$c2019$$dQ2$$eT1
000087594 592__ $$a1.317$$b2019
000087594 593__ $$aMedicine (miscellaneous)$$c2019$$dQ1
000087594 593__ $$aPhysical and Theoretical Chemistry$$c2019$$dQ1
000087594 593__ $$aComputer Science Applications$$c2019$$dQ1
000087594 593__ $$aInorganic Chemistry$$c2019$$dQ1
000087594 593__ $$aSpectroscopy$$c2019$$dQ1
000087594 593__ $$aOrganic Chemistry$$c2019$$dQ1
000087594 593__ $$aMolecular Biology$$c2019$$dQ2
000087594 593__ $$aCatalysis$$c2019$$dQ2
000087594 655_4 $$ainfo:eu-repo/semantics/review$$vinfo:eu-repo/semantics/publishedVersion
000087594 700__ $$0(orcid)0000-0002-4703-6620$$aLatorre-Pellicer, Ana$$uUniversidad de Zaragoza
000087594 700__ $$aLucia-Campos, Cristina$$uUniversidad de Zaragoza
000087594 700__ $$aGil-Salvador, Marta
000087594 700__ $$aAntoñanzas-Peréz, Rebeca$$uUniversidad de Zaragoza
000087594 700__ $$aGómez-Puertas, Paulino
000087594 700__ $$0(orcid)0000-0002-0902-387X$$aBueno-Lozano, Gloria$$uUniversidad de Zaragoza
000087594 700__ $$0(orcid)0000-0003-0170-7326$$aPuisac, Beatriz$$uUniversidad de Zaragoza
000087594 700__ $$0(orcid)0000-0003-3203-6254$$aPié, Juan$$uUniversidad de Zaragoza
000087594 7102_ $$11005$$2410$$aUniversidad de Zaragoza$$bDpto. Farmacología y Fisiolog.$$cÁrea Fisiología
000087594 7102_ $$11005$$2X$$aUniversidad de Zaragoza$$bDpto. Farmacología y Fisiolog.$$cProy. investigación DUA
000087594 7102_ $$11010$$2670$$aUniversidad de Zaragoza$$bDpto. Pediatría Radiol.Med.Fís$$cÁrea Pediatría
000087594 773__ $$g20, 24 (2019), 6124 [14 pp.]$$pInt. j. mol. sci.$$tInternational Journal of Molecular Sciences$$x1661-6596
000087594 8564_ $$s967531$$uhttps://zaguan.unizar.es/record/87594/files/texto_completo.pdf$$yVersión publicada
000087594 8564_ $$s101921$$uhttps://zaguan.unizar.es/record/87594/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
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000087594 951__ $$a2023-07-06-12:20:32
000087594 980__ $$aARTICLE