Molecular basis of D-bifunctional protein deficiency

Mol Cell Endocrinol. 2001 Jan 22;171(1-2):61-70. doi: 10.1016/s0303-7207(00)00388-9.


Peroxisomal disorders appear with a frequency of 1:5000 in newborns. They are caused either by peroxisomal assembly defects or by deficiencies of single peroxisomal enzymes. The phenotypes vary widely: affected humans may die very early in life within a few days to several months as a result of the impairment in essential peroxisomal functions as, for example, in Zellweger syndrome, or they may show only minor disabilities as is in acatalasemia. The deficiency of D-bifunctional protein, an enzyme involved in peroxisomal beta-oxidation of certain fatty acids and the synthesis of bile acids, causes a very severe, Zellweger-like phenotype. A number of different mutations in the gene coding for the enzyme were found in humans causing the total or partial loss of its enzymatic function. This paper gives a review of cases and their molecular basis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • 17-Hydroxysteroid Dehydrogenases*
  • 3-Hydroxyacyl CoA Dehydrogenases / deficiency*
  • 3-Hydroxyacyl CoA Dehydrogenases / genetics*
  • Animals
  • Enoyl-CoA Hydratase*
  • Frameshift Mutation
  • Gene Deletion
  • Humans
  • Hydro-Lyases / deficiency*
  • Hydro-Lyases / genetics*
  • Infant, Newborn
  • Multienzyme Complexes / deficiency*
  • Multienzyme Complexes / genetics*
  • Peroxisomal Multifunctional Protein-2
  • Point Mutation
  • Polymorphism, Genetic


  • Multienzyme Complexes
  • 17-Hydroxysteroid Dehydrogenases
  • 3-Hydroxyacyl CoA Dehydrogenases
  • Hydro-Lyases
  • Peroxisomal Multifunctional Protein-2
  • HSD17B4 protein, human
  • Enoyl-CoA Hydratase