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MLYCD  -  malonyl-CoA decarboxylase

Homo sapiens

Synonyms: MCD, Malonyl-CoA decarboxylase, mitochondrial, hMCD
 
 
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Disease relevance of MLYCD

 

Psychiatry related information on MLYCD

  • These self-reported scores were adjusted for response bias by the long version of the Marlowe-Crowne Social Desirability Scale (MCD) [5].
 

High impact information on MLYCD

  • Short-chain acyl-CoA dehydrogenase (SCADH; EC 1.3.99.2), MCADH, and isovaleryl-CoA dehydrogenase (IVDH; EC 1.3.99.10) activities were assayed with 100 microM [2,3-3H]butyryl-, -octanoyl-, and -isovaleryl-CoAs, respectively, in fibroblasts cultured from normal controls and MCD patients [6].
  • Without the artificial electron acceptor phenazine methosulfate (PMS), MCADH activity in fibroblast mitochondrial sonic supernatants (MS) was 54% of control in two MCD cell lines (P less than 0.05) [6].
  • Medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCADH; EC 1.3.99.3) deficiency (MCD) is an inborn error of beta-oxidation [6].
  • This targeting signal appears to be functional in vivo, since the distribution of MCD enzymatic activity in rat liver homogenates-as measured by means of subcellular fractionation-strongly suggests that MCD is localized to peroxisomes in addition to the mitochondrial localization reported elsewhere [7].
  • We characterized a 2.1-kb human cDNA with a 1362-bp (454-amino acid) open reading frame showing 70.3% amino acid identity to goose malonyl-CoA decarboxylase (MCD) [7].
 

Chemical compound and disease context of MLYCD

 

Biological context of MLYCD

 

Anatomical context of MLYCD

  • Fibroblast cell lines were available from eight of these patients and two previously reported patients with homozygous MLYCD mutations [2].
  • Immunocytochemical analysis of MLYCD-expressing patient cell lines showed apparent intracellular mislocalization [2].
  • The abundance of peroxisome proliferator-activated receptor (PPAR)gamma coactivator-1alpha (PGC-1alpha), a regulator of transcription that has been linked to the mediation of MCD expression by PPARalpha, was also increased (3-fold) [16].
  • Additional support for this hypothesis comes from our observation that MCD mRNA is most abundant in cardiac and skeletal muscles, tissues in which cytoplasmic malonyl-CoA is a potent inhibitor of mitochondrial fatty acid oxidation and which derive significant amounts of energy from fatty acid oxidation [13].
  • Malonyl-CoA decarboxylase in rat brain mitochondria [17].
 

Associations of MLYCD with chemical compounds

  • Exercise training decreases the concentration of malonyl-CoA and increases the expression and activity of malonyl-CoA decarboxylase in human muscle [16].
  • Fibroblasts from patients with MCD are unable to increase HCS mRNA in response to biotin unless the vitamin concentration is raised 100-fold, in keeping with mutations that cause a reduced affinity for biotin by the mutant enzyme [3].
  • This assignment is further supported by features in the MCD spectrum whose intensity correlates with an EPR signal associated with uncoupled type 3 Cu(II) sites [18].
  • HCS and carboxylase mRNA levels in normal and MCD fibroblasts and HepG2 cells can be restored by the addition of the cGMP analogue, 8-Br-cGMP, and can be abolished by the addition of inhibitors of the soluble form of guanylate cyclase [3].
  • Treatment of 832/13 cells with AdCMV-MCD Delta 5 completely blocked the glucose-induced rise in malonyl-CoA and attenuated the inhibitory effect of glucose on fatty acid oxidation [19].
 

Regulatory relationships of MLYCD

 

Other interactions of MLYCD

 

Analytical, diagnostic and therapeutic context of MLYCD

References

  1. Cloning and mutational analysis of human malonyl-coenzyme A decarboxylase. Gao, J., Waber, L., Bennett, M.J., Gibson, K.M., Cohen, J.C. J. Lipid Res. (1999) [Pubmed]
  2. MLYCD mutation analysis: evidence for protein mistargeting as a cause of MLYCD deficiency. Wightman, P.J., Santer, R., Ribes, A., Dougherty, F., McGill, N., Thorburn, D.R., FitzPatrick, D.R. Hum. Mutat. (2003) [Pubmed]
  3. Holocarboxylase synthetase is an obligate participant in biotin-mediated regulation of its own expression and of biotin-dependent carboxylases mRNA levels in human cells. Solórzano-Vargas, R.S., Pacheco-Alvarez, D., León-Del-Río, A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  4. Incidence and clinical significance of multiple consecutive, appropriate, high-energy discharges in patients with implanted cardioverter-defibrillators. Villacastín, J., Almendral, J., Arenal, A., Albertos, J., Ormaetxe, J., Peinado, R., Bueno, H., Merino, J.L., Pastor, A., Medina, O., Tercedor, L., Jiménez, F., Delcán, J.L. Circulation (1996) [Pubmed]
  5. A study of male veterans' beliefs toward domestic violence in a batterers intervention program. Craig, M.E., Robyak, J., Torosian, E.J., Hummer, J. Journal of interpersonal violence. (2006) [Pubmed]
  6. Catalytic defect of medium-chain acyl-coenzyme A dehydrogenase deficiency. Lack of both cofactor responsiveness and biochemical heterogeneity in eight patients. Amendt, B.A., Rhead, W.J. J. Clin. Invest. (1985) [Pubmed]
  7. The molecular basis of malonyl-CoA decarboxylase deficiency. FitzPatrick, D.R., Hill, A., Tolmie, J.L., Thorburn, D.R., Christodoulou, J. Am. J. Hum. Genet. (1999) [Pubmed]
  8. Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency. Dupuis, L., Leon-Del-Rio, A., Leclerc, D., Campeau, E., Sweetman, L., Saudubray, J.M., Herman, G., Gibson, K.M., Gravel, R.A. Hum. Mol. Genet. (1996) [Pubmed]
  9. Inhibition of erythromycin synthesis by disruption of malonyl-coenzyme A decarboxylase gene eryM in Saccharopolyspora erythraea. Hsieh, Y.J., Kolattukudy, P.E. J. Bacteriol. (1994) [Pubmed]
  10. Biotin-responsive immunoregulatory dysfunction in multiple carboxylase deficiency. Fischer, A., Munnich, A., Saudubray, J.M., Mamas, S., Coudé, F.X., Charpentier, C., Dray, F., Frézal, J., Griscelli, C. J. Clin. Immunol. (1982) [Pubmed]
  11. Serum IgE in primary glomerular diseases and its clinical significance. Shu, K.H., Lian, J.D., Yang, Y.F., Lu, Y.S., Wang, J.Y. Nephron (1988) [Pubmed]
  12. Holocarboxylase synthetase deficiency: report of a case with onset in late infancy. Touma, E., Suormala, T., Baumgartner, E.R., Gerbaka, B., Ogier de Baulny, H., Loiselet, J. J. Inherit. Metab. Dis. (1999) [Pubmed]
  13. MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonyl-CoA decarboxylase deficiency. Sacksteder, K.A., Morrell, J.C., Wanders, R.J., Matalon, R., Gould, S.J. J. Biol. Chem. (1999) [Pubmed]
  14. Assay of the activity of malonyl-coenzyme A decarboxylase by gas chromatography-mass spectrometry. Wang, X., Stanley, W.C., Brunengraber, H., Kasumov, T. Anal. Biochem. (2007) [Pubmed]
  15. Autosomal dominant medullary cystic disease: a disorder with variable clinical pictures and exclusion of linkage with the NPH1 locus. Scolari, F., Ghiggeri, G.M., Casari, G., Amoroso, A., Puzzer, D., Caridi, G.L., Valzorio, B., Tardanico, R., Vizzardi, V., Savoldi, S., Viola, B.F., Bossini, N., Prati, E., Gusmano, R., Maiorca, R. Nephrol. Dial. Transplant. (1998) [Pubmed]
  16. Exercise training decreases the concentration of malonyl-CoA and increases the expression and activity of malonyl-CoA decarboxylase in human muscle. Kuhl, J.E., Ruderman, N.B., Musi, N., Goodyear, L.J., Patti, M.E., Crunkhorn, S., Dronamraju, D., Thorell, A., Nygren, J., Ljungkvist, O., Degerblad, M., Stahle, A., Brismar, T.B., Andersen, K.L., Saha, A.K., Efendic, S., Bavenholm, P.N. Am. J. Physiol. Endocrinol. Metab. (2006) [Pubmed]
  17. Malonyl-CoA decarboxylase in rat brain mitochondria. Kim, Y.S., Kolattukudy, P.E., Boos, A. Int. J. Biochem. (1979) [Pubmed]
  18. Low-temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site. Allendorf, M.D., Spira, D.J., Solomon, E.I. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  19. Overexpression of a modified human malonyl-CoA decarboxylase blocks the glucose-induced increase in malonyl-CoA level but has no impact on insulin secretion in INS-1-derived (832/13) beta-cells. Mulder, H., Lu, D., Finley, J., An, J., Cohen, J., Antinozzi, P.A., McGarry, J.D., Newgard, C.B. J. Biol. Chem. (2001) [Pubmed]
  20. Expression of genes regulating Malonyl-CoA in human skeletal muscle. Pender, C., Trentadue, A.R., Pories, W.J., Dohm, G.L., Houmard, J.A., Youngren, J.F. J. Cell. Biochem. (2006) [Pubmed]
  21. Myocardial carnitine palmitoyltransferase I as a target for oxidative modification in inflammation and sepsis. Eaton, S., Fukumoto, K., Stefanutti, G., Spitz, L., Zammit, V.A., Pierro, A. Biochem. Soc. Trans. (2003) [Pubmed]
  22. Brain abnormalities in a case of malonyl-CoA decarboxylase deficiency. de Wit, M.C., de Coo, I.F., Verbeek, E., Schot, R., Schoonderwoerd, G.C., Duran, M., de Klerk, J.B., Huijmans, J.G., Lequin, M.H., Verheijen, F.W., Mancini, G.M. Mol. Genet. Metab. (2006) [Pubmed]
  23. Spectroscopic properties and electronic structure of low-spin Fe(III)-alkylperoxo complexes: homolytic cleavage of the O-O bond. Lehnert, N., Ho, R.Y., Que, L., Solomon, E.I. J. Am. Chem. Soc. (2001) [Pubmed]
  24. Tandem mass spectrometric determination of malonylcarnitine: diagnosis and neonatal screening of malonyl-CoA decarboxylase deficiency. Santer, R., Fingerhut, R., Lässker, U., Wightman, P.J., Fitzpatrick, D.R., Olgemöller, B., Roscher, A.A. Clin. Chem. (2003) [Pubmed]
  25. Kinetic, spectroscopic, and structural investigations of the soybean lipoxygenase-1 first-coordination sphere mutant, Asn694Gly. Segraves, E.N., Chruszcz, M., Neidig, M.L., Ruddat, V., Zhou, J., Wecksler, A.T., Minor, W., Solomon, E.I., Holman, T.R. Biochemistry (2006) [Pubmed]
 
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