Cloning and mutational analysis of human malonyl-coenzyme A decarboxylase

Journal of Lipid Research

Volumn 40, Issue 1, 1999, Pages 178-182

  Gao, Jimin ^a   Waber, Lewis ^b   Bennett, Michael J ^b   Michael Gibson, K ^c   Cohen, Jonathan C ^a,b  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

Frameshift mutation; Inborn errors; Metabolism; Microbodies; Mitochondria

Indexed keywords

CARBOXYLYASE; COMPLEMENTARY DNA; MALONYL COENZYME A; MALONYL COENZYME A DECARBOXYLASE; UNCLASSIFIED DRUG;

ARTICLE; CASE REPORT; CATALYSIS; CHROMOSOMAL LOCALIZATION; CONTROLLED STUDY; DISEASE ASSOCIATION; DNA DETERMINATION; DNA SEQUENCE; ENZYME ACTIVITY; ENZYME DEFICIENCY; EXON; GENE MUTATION; GENE SEQUENCE; HUMAN; INTRON; MALE; METABOLIC DISORDER; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CARBOXY-LYASES; CARDIOMYOPATHY, HYPERTROPHIC; CHROMOSOME MAPPING; CHROMOSOMES, HUMAN, PAIR 16; CLONING, MOLECULAR; DNA MUTATIONAL ANALYSIS; DNA, COMPLEMENTARY; GEESE; HUMANS; INFANT; MALE; MALONATES; METABOLISM, INBORN ERRORS; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY;

EID: 0032895659     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (18)

1. Kim, Y. S., and P. E. Kolattukudy. 1978. Malonyl-CoA decarboxylase from the mammary gland of lactating rat. Purification, properties and subcellular localization. Biochim. Biophys. Acta. 531: 187-196.
2. Kim, Y. S., and P. E. Kolattukudy. 1978. Malonyl-CoA decarboxylase from the uropygial gland of waterfowl: purification, properties, immunological comparison, and role in regulating the synthesis of multimethyl-branched fatty acids. Arch. Biochem. Biophys. 190: 585-597.
3. Kim, Y. S., and P. E. Kolattukudy. 1978. 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. Biophis. 190: 234-246.
4. Kim, Y. S., P. E. Kolattukudy, and A. Boos. 1979. Malonyl-CoA decarboxylase from Mycobacterium tuberculosis and Pseudomonas fluorescens. Arch. Biochem. Biophys. 196: 543-551.
5. Scholte, H. R. 1969. The intracellular and intramitochondrial distribution of malonyl-CoA decarboxylase and propionyl-CoA carboxylase in rat liver. Biochim. Biophys. Acta. 178: 137-144.
6. Kim, Y. S., P. E. Kolattukudy, and A. Boos. 1979. Dual sites of occurrence of malonyl-CoA decarboxylase and their possible functional significance in avian tissues. Comp. Biochem. Physiol. [B.]. 62: 443-447.
7. Kim, Y. S., P. E. Kolattukudy, and A. Boos. 1979. Malonyl-CoA decarboxylase in rat brain mitochondria. Int. J. Biochem. 10: 551-555.
8. Brown, G. K., R. D. Scholem, A. Bankier, and D. M. Danks. 1984. Malonyl coenzyme A decarboxylase deficiency. J. Inherit. Metab. Dis. 7: 21-26.
9. Haan, E. A., R. D. Scholem, H. B. Croll, and G. K. Brown. 1986. Malonyl coenzyme A decarboxylase deficiency. Clinical and biochemical findings in a second child with a more severe enzyme defect. Eur. J. Pediatr. 144: 567-570.
10. MacPhee, G. B., R. W. Logan, J. S. Mitchell, D. W. Howells, E. Tsotsis, and D. R. Thorburn. 1993. Malonyl coenzyme A decarboxylase deficiency. Arch. Dis. Child. 69: 433-436.
11. Matalon, R., K. Michaels, R. Kaul, V. Whitman, J. Rodriguez-Novo, S. Goodman, and D. Thorburn. 1993. Malonic aciduria and cardiomyopathy. J. Inherit. Metab. Dis. 16: 571-573.
12. Krawinkell M. B., H. D. Oldigs, R. Santer, W. Lehnert, U. Wendel, and J. Schaub. 1994. Association of malonyl-CoA decarboxylase deficiency and heterozygote state for haemoglobin C disease. J. Inherit. Metab. Dis. 17: 636-637.
13. Yano, S., I., Sweetman, D. R. Thorburn, S. Mofidi, and J. C. Williams. 1997. A new case of malonyl coenzyme A decarboxylase deficiency presenting with cardiomyopathy. Eur. J. Pediatr. 156: 382-383.
14. Jang, S. H., T. M. Cheesbrough, and P. E. Kolattukudy. 1989. Molecular cloning, nucleotide sequence, and tissue distribution of malonyl-CoA decarboxylase. J. Biol. Chem. 264: 3500-3505.
15. Aminozzi, P. A., L. Segall, M. Prentki, J. D. McGarry, and C. B. Newgard. 1998. Molecular or pharmacologic perturbation of the link between glucose and lipid metabolism is without effect on glucose-stimulated insulin secretion. A re-evaluation of the long-chain acyl-CoA hypothesis. J. Biol. Chem. 273: 16146-16154.
16. Courchesne-Smith, C., S. H. Jang, Q. Shi, J. DeWille, G. Sasaki, and P. E. Kolattukudy. 1992. Cytoplasmic accumulation of a normally mitochondrial malonyl-CoA decarboxylase by the use of an alternate transcription start site. Arch. Biochem. Biophys. 298: 576-586.
17. Kozak, M. 1996. Interpreting cDNA sequences: some insights from studies on translation. Mamm. Genome. 7: 563-574.
18. McNew, J. A., and J. M. Goodman. 1996. The targeting and assembly of peroxisomal proteins: some old rules do not apply. Trends Biochem. Sci. 21: 54-58.