Skip to main content
SpringerLink
Log in

Malonyl coenzyme a decarboxylase deficiency

  • Published:
Journal of Inherited Metabolic Disease

Abstract

A patient is described with a deficiency of the mitochondrial enzyme, malonyl CoA decarboxylase — an inborn error of metabolism not recognized previously. The enzyme defect was first suspected because of persistent excretion of malonic and methylmalonic acids in urine in a child with repeated episodes of vomiting, some requiring hospitalization. Disturbances of lipid metabolism were demonstrated.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Ahmad, P. M., Russell, T. R. and Ahmad, F. Increase in fatty acid synthetase content of 3T3-L cells undergoing spontaneous and chemically induced differentiation to adipocytes.Biochem. J. 182 (1979) 509–514

    PubMed  Google Scholar 

  • Babior, B. M., Woodams, A. D. and Brodie, J. D. Cleavage of coenzyme B12 by methylmalonyl coenzyme A mutase.J. Biol. Chem. 248 (1973) 1445–1450

    PubMed  Google Scholar 

  • Bressler, R. and Wakil, S. J. Studies on the mechanism of fatty acid synthesis IX. The conversion of malonyl coenzyme A to long chain fatty acids.J. Biol. Chem. 236 (1961) 1643–1651

    Google Scholar 

  • Chen, T. R.In situ detection of mycoplasma contamination in cell cultures by fluorescent Hoechst 33258 stain.Exp. Cell Res. 104 (1977) 252–262

    Google Scholar 

  • Fox, R. M. A simple incubation flask for14CO2 collection.Anal. Biochem. 41 (1971) 578–580

    PubMed  Google Scholar 

  • Hülsmann, W. C. On the synthesis of malonyl coenzyme A in rabbit heart sarcosomes.Biochim. Biophys. Acta 125 (1966) 397–400

    Google Scholar 

  • Koeppen, A. H., Mitzen, E. J. and Ammoumi, A. A. Malonate metabolism in rat brain mitochondria.Biochemistry 13 (1974) 3589–3595

    PubMed  Google Scholar 

  • Krebs, H. A. and Henseleit, K. Untersuchungen über die Harnstoffbildung im Tierkörper.Hoppe Seyler's Z. Physiol. Chem. 210 (1932) 33–66

    Google Scholar 

  • Landriscina, C., Gnoni, G. V. and Quagliariello, E. Properties of malonyl-CoA decarboxylase and its relation with malonyl CoA incorporation into fatty acids by rat liver mitochondria.Eur. J. Biochem. 19 (1971) 573–580

    PubMed  Google Scholar 

  • Lane, M. D., Halenz, D. R., Kosow, D. P. and Hegre, C. S. Further studies on mitochondrial propionyl CoA carboxylase.J. Biol. Chem. 235 (1960) 3082–3086

    PubMed  Google Scholar 

  • Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. Protein measurement with the folin phenol reagent.J. Biol. Chem. 193 (1951) 265–275

    PubMed  Google Scholar 

  • Morrow, G. (III), Mahoney, M. J., Mathews, C. and Lebowitz, J. Studies of methylmalonyl coenzyme A carbonylmutase activity in methylmalonic acidaemia. 1. Correlation of clinical, hepatic, and fibroblast data.Pediatr. Res. 9 (1975) 641–644

    PubMed  Google Scholar 

  • Rosenberg, L. E. Disorders of propionate and methylmalonate metabolism. In Stanbury, J. B., Wyngaarden, J. B., Fredrickson, D. J., Goldstein, J. L. and Brown, M. S.The Metabolic Basis of Inherited Disease, 5th Edn, McGraw-Hill, New York, 1983, pp. 474–497

    Google Scholar 

  • Scholte, H. R. The intracellular and intramitochondrial distribution of malonyl CoA decarboxylase and propionyl CoA carboxylase in rat liver.Biochim. Biophys. Acta 178 (1969) 137–144

    PubMed  Google Scholar 

  • Stjernholm, R. L., Noble, E. P., Dimitrov, N. V. and Kellermeyer, R. W. Differentiation of normal and leukemic leukocytes into three groups by propionate metabolism.J. Reticuloendothelial Soc. 8 (1970) 446–457

    Google Scholar 

  • Whitaker, T. R. and Giorgio, A. J. A direct radioassay of methylmalonyl coenzyme A mutase using enzymatically synthesisedD,l-[3-14C]methylmalonyl CoA.Anal. Biochem. 52 (1973) 522–532

    PubMed  Google Scholar 

  • Yu Sam Kim and Kolattukudy, P. E. Malonyl CoA decarboxylase from the mammary gland of lactating rat.Biochim. Biophys. Acta 531 (1978a) 187–196

    PubMed  Google Scholar 

  • Yu Sam Kim and Kolattukudy, P. E. Purification and properties of malonyl CoA decarboxylase from rat liver mitochondria and its immunological comparison with the enzymes from rat brain, heart and mammary gland.Arch. Biochem. Biophys. 190 (1978b) 234–246

    PubMed  Google Scholar 

  • Zuurendonk, P. F. and Tager, J. M. Rapid separation of particulate components and soluble cytoplasm of isolated rat liver cells.Biochim. Biophys. Acta 333 (1974) 393–399

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Paediatrics, University of Melbourne and Birth Defects Research Institute, Royal Children's Hospital, 3052, Parkville, Victoria, Australia

    G. K. Brown, R. D. Scholem, A. Bankier & D. M. Danks

Authors
  1. G. K. Brown
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. R. D. Scholem
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. A. Bankier
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. D. M. Danks
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Brown, G.K., Scholem, R.D., Bankier, A. et al. Malonyl coenzyme a decarboxylase deficiency. J Inherit Metab Dis 7, 21–26 (1984). https://doi.org/10.1007/BF01805615

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01805615

Keywords

Search

Navigation