Desulfation of Tyrosine-O-sulfated Peptides by Some Eukaryotic Sulfatases

Three mammalian and eight non-mammalian arylsulfatases were investigated for their activities toward tyrosine-O-sulfate (TyrS) in peptides. None of the mammalian arylsulfatases exhibited detectable activities toward TyrS-containing peptides. Of the non-mammalian arylsulfatases tested, Types VII, VII...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1996-01, Vol.60 (1), p.137-138
Main Authors: Suiko, Masahito, Tojo, Tamaki, Prasantha Fernando, P. H., Sakakibara, Yoichi, Kawano, Jun-ichi, Liu, Ming-Cheh
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
arylsulfatase
Biological and medical sciences
Biotechnology
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
modifications
Peptides - metabolism
post-translational
Protein Biosynthesis - genetics
Sulfatases - chemistry
Tyrosine - analogs & derivatives
Tyrosine - chemistry
tyrosine sulfation
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Summary:Three mammalian and eight non-mammalian arylsulfatases were investigated for their activities toward tyrosine-O-sulfate (TyrS) in peptides. None of the mammalian arylsulfatases exhibited detectable activities toward TyrS-containing peptides. Of the non-mammalian arylsulfatases tested, Types VII, VIII, and H-1, 2, and 5 displayed strong activity on endo-TvrS residues. The prokaryotic sulfatase, Type VI, was active only on free TyrS and N-terminal TyrS of Leu-enkephalin. All the sulfatases were active on p-nitrophenyl sulfate and p-nitrocatechol sulfate.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.60.137