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

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

doi:10.1016/S0006-291X(88)80035-4

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

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

Hopwood Centre For Neurobiology

Research output: Contribution to journal › Article › peer-review

40 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 language	English
Pages (from-to)	218-224
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	157
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(88)80035-4
Publication status	Published or Issued - 30 Nov 1988

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/S0006-291X(88)80035-4

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@article{e38e8ede37504047a0dde4dccb750186,

title = "Human glucosamine-6-sulfatase cDNA reveals homology with steroid sulfatase",

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.",

author = "Robertson, {Daniel A.} and Craig Freeman and Nelson, {Paul V.} and Morris, {C. Phillip} and Hopwood, {John J.}",

note = "Funding Information: We would like to thank L.J. Shapiro, Department of Pediatrics, UCLA School of Medicine for helpful discussions on STS homology, P.R. Clements, Department of Chemical Pathology, Adelaide Children's Hospital for advice on N-terminal sequencing of G6S and G. Howlett, Department of Biochemistry, University of Melbourne for providing the human liver cDNA library. This work was supported by The Australian National Health and Medical Research Council and the Adelaide Chidren's Hospital Research Foundation.",

year = "1988",

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day = "30",

doi = "10.1016/S0006-291X(88)80035-4",

language = "English",

volume = "157",

pages = "218--224",

journal = "Biochemical and Biophysical Research Communications",

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TY - JOUR

T1 - Human glucosamine-6-sulfatase cDNA reveals homology with steroid sulfatase

AU - Robertson, Daniel A.

AU - Freeman, Craig

AU - Nelson, Paul V.

AU - Morris, C. Phillip

AU - Hopwood, John J.

N1 - Funding Information: We would like to thank L.J. Shapiro, Department of Pediatrics, UCLA School of Medicine for helpful discussions on STS homology, P.R. Clements, Department of Chemical Pathology, Adelaide Children's Hospital for advice on N-terminal sequencing of G6S and G. Howlett, Department of Biochemistry, University of Melbourne for providing the human liver cDNA library. This work was supported by The Australian National Health and Medical Research Council and the Adelaide Chidren's Hospital Research Foundation.

PY - 1988/11/30

Y1 - 1988/11/30

N2 - 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.

AB - 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.

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U2 - 10.1016/S0006-291X(88)80035-4

DO - 10.1016/S0006-291X(88)80035-4

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AN - SCOPUS:0024243887

SN - 0006-291X

VL - 157

SP - 218

EP - 224

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

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

Abstract

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