Tyrosine Sulfation as a Protein Post-Translational Modification

Bibliographic Details
Title: Tyrosine Sulfation as a Protein Post-Translational Modification
Authors: Yuh-Shyong Yang, Chen-Chu Wang, Bo-Han Chen, You-Hua Hou, Kuo-Sheng Hung, Yi-Chih Mao
Source: Molecules, Vol 20, Iss 2, Pp 2138-2164 (2015)
Publisher Information: MDPI AG, 2015.
Publication Year: 2015
Collection: LCC:Organic chemistry
Subject Terms: sulfate, organic sulfate, post-translational modification (PTM), protein tyrosine sulfation (PTS), tyrosylprotein sulfotransferase (TPST), 3'-phosphoadenosine 5'-phosphosulfate (PAPS), Organic chemistry, QD241-441
More Details: Integration of inorganic sulfate into biological molecules plays an important role in biological systems and is directly involved in the instigation of diseases. Protein tyrosine sulfation (PTS) is a common post-translational modification that was first reported in the literature fifty years ago. However, the significance of PTS under physiological conditions and its link to diseases have just begun to be appreciated in recent years. PTS is catalyzed by tyrosylprotein sulfotransferase (TPST) through transfer of an activated sulfate from 3'-phosphoadenosine-5'-phosphosulfate to tyrosine in a variety of proteins and peptides. Currently, only a small fraction of sulfated proteins is known and the understanding of the biological sulfation mechanisms is still in progress. In this review, we give an introductory and selective brief review of PTS and then summarize the basic biochemical information including the activity and the preparation of TPST, methods for the determination of PTS, and kinetics and reaction mechanism of TPST. This information is fundamental for the further exploration of the function of PTS that induces protein-protein interactions and the subsequent biochemical and physiological reactions.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1420-3049
Relation: http://www.mdpi.com/1420-3049/20/2/2138; https://doaj.org/toc/1420-3049
DOI: 10.3390/molecules20022138
Access URL: https://doaj.org/article/593f8554d843441ca8b89ba594aa6c59
Accession Number: edsdoj.593f8554d843441ca8b89ba594aa6c59
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  Data: Tyrosine Sulfation as a Protein Post-Translational Modification
– Name: Author
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  Data: <searchLink fieldCode="AR" term="%22Yuh-Shyong+Yang%22">Yuh-Shyong Yang</searchLink><br /><searchLink fieldCode="AR" term="%22Chen-Chu+Wang%22">Chen-Chu Wang</searchLink><br /><searchLink fieldCode="AR" term="%22Bo-Han+Chen%22">Bo-Han Chen</searchLink><br /><searchLink fieldCode="AR" term="%22You-Hua+Hou%22">You-Hua Hou</searchLink><br /><searchLink fieldCode="AR" term="%22Kuo-Sheng+Hung%22">Kuo-Sheng Hung</searchLink><br /><searchLink fieldCode="AR" term="%22Yi-Chih+Mao%22">Yi-Chih Mao</searchLink>
– Name: TitleSource
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  Data: Molecules, Vol 20, Iss 2, Pp 2138-2164 (2015)
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  Data: MDPI AG, 2015.
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  Label: Publication Year
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  Data: 2015
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  Data: LCC:Organic chemistry
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  Data: <searchLink fieldCode="DE" term="%22sulfate%22">sulfate</searchLink><br /><searchLink fieldCode="DE" term="%22organic+sulfate%22">organic sulfate</searchLink><br /><searchLink fieldCode="DE" term="%22post-translational+modification+%28PTM%29%22">post-translational modification (PTM)</searchLink><br /><searchLink fieldCode="DE" term="%22protein+tyrosine+sulfation+%28PTS%29%22">protein tyrosine sulfation (PTS)</searchLink><br /><searchLink fieldCode="DE" term="%22tyrosylprotein+sulfotransferase+%28TPST%29%22">tyrosylprotein sulfotransferase (TPST)</searchLink><br /><searchLink fieldCode="DE" term="%223'-phosphoadenosine+5'-phosphosulfate+%28PAPS%29%22">3'-phosphoadenosine 5'-phosphosulfate (PAPS)</searchLink><br /><searchLink fieldCode="DE" term="%22Organic+chemistry%22">Organic chemistry</searchLink><br /><searchLink fieldCode="DE" term="%22QD241-441%22">QD241-441</searchLink>
– Name: Abstract
  Label: Description
  Group: Ab
  Data: Integration of inorganic sulfate into biological molecules plays an important role in biological systems and is directly involved in the instigation of diseases. Protein tyrosine sulfation (PTS) is a common post-translational modification that was first reported in the literature fifty years ago. However, the significance of PTS under physiological conditions and its link to diseases have just begun to be appreciated in recent years. PTS is catalyzed by tyrosylprotein sulfotransferase (TPST) through transfer of an activated sulfate from 3'-phosphoadenosine-5'-phosphosulfate to tyrosine in a variety of proteins and peptides. Currently, only a small fraction of sulfated proteins is known and the understanding of the biological sulfation mechanisms is still in progress. In this review, we give an introductory and selective brief review of PTS and then summarize the basic biochemical information including the activity and the preparation of TPST, methods for the determination of PTS, and kinetics and reaction mechanism of TPST. This information is fundamental for the further exploration of the function of PTS that induces protein-protein interactions and the subsequent biochemical and physiological reactions.
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  Data: http://www.mdpi.com/1420-3049/20/2/2138; https://doaj.org/toc/1420-3049
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  Data: 10.3390/molecules20022138
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        Value: 10.3390/molecules20022138
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      – Text: English
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        PageCount: 27
        StartPage: 2138
    Subjects:
      – SubjectFull: sulfate
        Type: general
      – SubjectFull: organic sulfate
        Type: general
      – SubjectFull: post-translational modification (PTM)
        Type: general
      – SubjectFull: protein tyrosine sulfation (PTS)
        Type: general
      – SubjectFull: tyrosylprotein sulfotransferase (TPST)
        Type: general
      – SubjectFull: 3'-phosphoadenosine 5'-phosphosulfate (PAPS)
        Type: general
      – SubjectFull: Organic chemistry
        Type: general
      – SubjectFull: QD241-441
        Type: general
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      – TitleFull: Tyrosine Sulfation as a Protein Post-Translational Modification
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            NameFull: Yuh-Shyong Yang
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            NameFull: Chen-Chu Wang
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            NameFull: Bo-Han Chen
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            NameFull: Kuo-Sheng Hung
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