Hostname: page-component-745bb68f8f-b6zl4 Total loading time: 0 Render date: 2025-01-12T18:35:10.218Z Has data issue: false hasContentIssue false
  • English
  • Français

Malonyl coenzyme A decarboxylase deficiency with a novel mutation

Part of: Metabolic

Published online by Cambridge University Press:  22 March 2021

Cigdem S. Kasapkara Open the ORCID record for Cigdem S. Kasapkara [Opens in a new window] ,
Burcu Civelek Ürey ,
Ahmet C. Ceylan ,
Özlem Ünal Uzun  and
Ibrahim İ. Çetin
Cigdem S. Kasapkara*
Affiliation:
Department of Pediatric Metabolism, Ankara Yildirim Beyazit University, Ankara City Hospital, Ankara, Turkey
Burcu Civelek Ürey
Affiliation:
Department of Pediatric Metabolism, Ankara City Hospital, Ankara, Turkey
Ahmet C. Ceylan
Affiliation:
Department of Genetics, Ankara Yildirim Beyazit University, Ankara City Hospital, Ankara, Turkey
Özlem Ünal Uzun
Affiliation:
Department of Pediatric Metabolism, Ankara City Hospital, Ankara, Turkey
Ibrahim İ. Çetin
Affiliation:
Department of Pediatric Cardiology, Ankara Yildirim Beyazit University, Ankara City Hospital, Ankara, Turkey
*
Author for correspondence: Dr C. S. Kasapkara, Department of Pediatric Metabolism, Ankara Yildirim Beyazit University, Ankara City Hospital, Bilkent Street. Number: 1 Çankaya, Ankara, Turkey. Tel: +903125526000. E-mail: cskasapkara@gmail.com
Get access Rights & Permissions [Opens in a new window]

Abstract

Malonyl-CoA, a product of acetyl-CoA carboxylase is a metabolic intermediate in lipogenic tissues that include liver and adipose tissue, where it is involved in the de novo fatty acid synthesis and elongation. Malonyl-CoA decarboxylase (MLYCD, E.C.4.1.1.9), a 55-kDa enzyme catalyses the conversion of malonyl-CoA to acetyl-CoA and carbon dioxide, thus providing a route for disposal of malonyl-CoA from mitochondria and peroxisomes, whereas in the cytosol, the malonyl-CoA pool is regulated by the balance of MLYCD and acetyl-CoA carboxylase activities. So far, 34 cases with different MLYCD gene defects comprising point mutations, stop codons, and frameshift mutations have been reported in the literature. Here, we describe the follow-up of a patient affected by malonic aciduria upon neonatal onset. Molecular analysis showed novel homozygous mutations in the MLYCD gene. Our findings expand the number of reported cases and add a novel variant to the repertoire of MLYCD mutations.

Keywords

Dilated cardiomyopathyfatty acid oxidation defectMalonyl CoA decarboxylase deficiency
Type
Brief Report
Information
Cardiology in the Young , Volume 31 , Issue 9 , September 2021 , pp. 1535 - 1537
Check for updates
Copyright
© The Author(s), 2021. Published by Cambridge University Press

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Liu, H, Tan, D, Han, L, et al. A new case of malonyl-CoA decarboxylase deficiency with mild clinical features. Am J Med Genet A 2016; 170: 1347–1351.CrossRefGoogle Scholar
Chapel-Crespo, C, Gavrilov, D, Sowa, M, et al. Clinical, biochemical and molecular characteristics of malonyl-CoA decarboxylase deficiency and long-term follow-up of nine patients. Mol Genet Metab 2019; 128: 113–121.CrossRefGoogle ScholarPubMed
Lee, SH, Ko, JM, Song, MK, Song, J, Park, KS. A Korean child diagnosed with malonic aciduria harboring a novel start codon mutation following presentation with dilated cardiomyopathy. Mol Genet Genomic Med 2020; 8: e1379.CrossRefGoogle ScholarPubMed
Jammal Addin, MB, Young, D, McCarrison, S, Hunter, L. Dilated cardiomyopathy in a national paediatric population. Eur J Pediatr 2019; 178: 1229–1235.CrossRefGoogle Scholar
Polinati, PP, Valanne, L, Tyni, T. Malonyl-CoA decarboxylase deficiency: long-term follow-up of a patient new clinical features and novel mutations. Brain Dev 2015; 37: 107–113.CrossRefGoogle ScholarPubMed
Peng, J, Wu, LQ, Zhou, MX, Zhong, L, Yin, F. A case of malonyl-CoA decarboxylase deficiency: clinical and genetic study. Zhongguo Dang Dai Er Ke Za Zhi 2012; 14: 879–880.Google ScholarPubMed
Prada, CE, Jefferies, JL, Grenier, MA, et al. Malonyl coenzyme A decarboxylase deficiency: early dietary restriction and time course of cardiomyopathy. Pediatrics 2012; 130: e456–e460.CrossRefGoogle ScholarPubMed
Baertling, F, Mayatepek, E, Thimm, E, et al. Malonic aciduria: long-term follow-up of new patients detected by newborn screening. Eur J Pediatr 2014; 173: 1719–1722.CrossRefGoogle ScholarPubMed
Xue, J, Peng, J, Zhou, M, et al. Novel compound heterozygous mutation of MLYCD in a Chinese patient with malonic aciduria. Mol Genet Metab 2012; 105: 79–83.CrossRefGoogle Scholar
Ersoy, M, Akyol, MB, Ceylaner, S, Çakır Biçer, N. A novel frameshift mutation of malonyl-CoA decarboxylase deficiency: clinical signs and therapy response of a late-diagnosed case. Clin Case Rep 2017; 5: 1284–1288.CrossRefGoogle ScholarPubMed