Substitution of alanine543 with a threonine residue at the carboxy terminal end of the beta-chain is associated with thermolabile hexosaminidase B in a Jewish family of Oriental ancestry

Biochem Mol Med. 1995 Oct;56(1):31-6. doi: 10.1006/bmme.1995.1053.

Abstract

Thermolabile forms of the lysosomal enzyme beta-hexosaminidase B (Hex B), likely to result from different genetic defects, have been described. Ten individuals in five generations of a family of Oriental Jewish ancestry were identified biochemically as carriers of a thermolabile Hex B form. The beta-chain thermolability was found to be associated with the presence of a G --> A transition at nucleotide 1627 of the HEX B gene causing the substitution of Ala543 with a threonine. Oriental Jew whose Hex B was heat labile. Since thermolabile Hex B has been shown to occur more frequently among Jews of Oriental origin, the Ala543 --> Thr mutation may be the common mutation associated with beta-chain thermolability in this ethnic group.

MeSH terms

  • Alanine / chemistry*
  • Base Sequence
  • Chromatography, Ion Exchange
  • Exons
  • Female
  • Fibroblasts / enzymology
  • Hexosaminidase B
  • Hot Temperature
  • Humans
  • Iran
  • Jews / genetics*
  • Male
  • Molecular Sequence Data
  • Pedigree
  • Protein Denaturation
  • Threonine / chemistry*
  • beta-N-Acetylhexosaminidases / chemistry
  • beta-N-Acetylhexosaminidases / genetics*
  • beta-N-Acetylhexosaminidases / metabolism

Substances

  • Threonine
  • Hexosaminidase B
  • beta-N-Acetylhexosaminidases
  • Alanine