Skip Navigation


Journal of Biochemistry Advance Access originally published online on October 8, 2006
Journal of Biochemistry 2006 140(5):731-737; doi:10.1093/jb/mvj206
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
140/5/731    most recent
mvj206v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Mishiro, E.
Right arrow Articles by Suiko, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mishiro, E.
Right arrow Articles by Suiko, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Japanese Biochemical Society.

ARTICLE

Differential Enzymatic Characteristics and Tissue-Specific Expression of Human TPST-1 and TPST-2

Emi Mishiro1, Yoichi Sakakibara1, Ming-Cheh Liu2 and Masahito Suiko1,*

1 Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, University of Miyazaki, Miyazaki 889-2192; and 2 Biomedical Research Center, The University of Texas Health Center, Tyler, TX 75708, USA

* To whom correspondence should be addressed. Phone/Fax: +81-985-58-7215, E-mail: msuiko{at}cc.miyazaki-u.ac.jp

Protein tyrosine sulfation is emerging as a widespread post-translational modification in multicellular eukaryotes. The responsible enzyme, named tyrosylprotein sulfotransferase (TPST), catalyzes the sulfate transfer from 3'-phosphoadenosine 5'-phosphosulfate to tyrosine residues of proteins. Two distinct TPSTs, designated TPST-1 and TPST-2, had previously been identified. In the present study, we cloned human TPST-1 and TPST-2 expressed and characterized the recombinant enzymes using peptide substrates. These enzymes displayed distinct acidic pH optima and stimulatory effects of Mn2+. Additionally, the activity of TPST-2, but not TPST-1, was stimulated in the presence of Mg2+. Compared with TPST-2, TPST-1 displayed considerably lower Km and Vmax for the majority of the tested peptide substrates, implying their differential substrate specificity. Quantitative real-time PCR analysis showed that although the two TPSTs were co-expressed in all 20 human tissues examined, the levels of expression of TPST-1 and TPST-2 varied significantly among different tissues. These latter findings may imply distinct physiological functions of TPST-1 and TPST-2.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Am. J. Respir. Cell Mol. Bio.Home page
J. Liu, S. Louie, W. Hsu, K. M. Yu, H. B. Nicholas Jr., and G. L. Rosenquist
Tyrosine Sulfation Is Prevalent in Human Chemokine Receptors Important in Lung Disease
Am. J. Respir. Cell Mol. Biol., June 1, 2008; 38(6): 738 - 743.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.