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, VIII, and H-1, 2, and 5 displayed strong activity on endo-TyrS 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.
Suiko
M
M
Department of Biological Resource Sciences, Miyazaki University, Japan.
Tojo
T
T
Fernando
P H
PH
Sakakibara
Y
Y
Kawano
J
J
Liu
M C
MC
D010455:Peptides / Q000378:metabolism*; D014176:Protein Biosynthesis / Q000235:genetics; D013429:Sulfatases / Q000737:chemistry*; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000737:chemistry
D010455:Peptides; C005662:tyrosine O-sulfate; D014443:Tyrosine; D013429:Sulfatases