Human glucosamine-6-sulfatase cDNA reveals homology with steroid sulfatase

Daniel A. Robertson, Craig Freeman, Paul V. Nelson, C. Phillip Morris, John J. Hopwood

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

Glucosamine-6-sulfatase is a lysosomal enzyme which degrades glycosaminoglycans and is deficient in mucopolysaccharidosis type IIID. Human liver contains two major active forms of glucosamine-6-sulfatase, form A which has a single 78 kDa polypeptide and form B which has two polypeptides of 48 kDa and 32 kDa. A 1761 base pair cDNA clone encoding the complete 48 kDa polypeptide of form B was isolated. Form A is shown to be processed to form B with the 48 kDa polypeptide C-terminal to the 32 kDa polypeptide, and it is shown that C-terminal processing is limited to a region of thirty amino acids. The glucosamine-6-sulfatase sequence reveals homology with steroid sulfatase, a microsomal enzyme.

Original languageEnglish
Pages (from-to)218-224
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume157
Issue number1
DOIs
Publication statusPublished or Issued - 30 Nov 1988

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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