Skip Navigation

This Article
Right arrow Full Text (PDF)
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 YOSHIMOTO, T.
Right arrow Articles by TSURU, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by YOSHIMOTO, T.
Right arrow Articles by TSURU, D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1982, Vol. 91, No. 6 1899-1906
© 1982 Japanese Biochemical Society

research-article

Proline-Specific Dipeptidyl Aminopeptidase from Flavobacterium meningosepticum1

Tadashi YOSHIMOTO, Faculty of Pharmaceutical Sciences and Daisuke TSURU, Faculty of Pharmaceutical Sciences

Nagasaki University Bunkyo-machi, Nagasaki, Nagasaki 852

A proline-specific dipeptidyl aminopeptidase was highly purified from cell-free extract of Flavobacterium meningosepticum by a series of column chromatographies on DEAE-Sephadex A-50, Sephadex G-150, hydroxyapatite, and a second gel filtration on Sephadex G-150. The enzyme was most active at pH 7.4–7.8 for both Gly-Pro-ß-naphthylamide (Gly-Pro-2-NNap) and Gly-Pro-p-nitroanilide (Gly-Pro-pNA) and was stable between pH 7 and 9.5. The enzyme was markedly inhibited by diisopropylphosphofluoridate (DFP) and mercury ion but not by sulfhydryl-blocking reagents and metal chelators. The molecular weight of the enzyme was about 160,000 as judged by the gel filtration method and the subunit molecular weight was estimated to be 75,000 by sodium dodecyl sulfate (SDS)-gel electropho-resis, suggesting a dimeric form of the native enzyme. The isoelectric point was at pH 9.5. The enzyme hydrolyzed peptides and peptide amides at the carboxyl side of a proline residue penultimate to the amino-terminal amino acid, as did post-proline dipeptidyl aminopeptidases from various mammals. However, antiserum raised against post-proline dipeptidyl aminopeptidase from porcine kidney did not cross-react with the Flavobacterium dipeptidyl aminopeptidase.

1This work was supported in part by grants from the Ministry of Education, Science and Culture of Japan, the Mishima Kaiun Memorial Foundation and the Applied Enzyme Foundation of Japan.


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
 J. Bacteriol.Home page
Y. Nakajima, K. Ito, T. Toshima, T. Egawa, H. Zheng, H. Oyama, Y.-F. Wu, E. Takahashi, K. Kyono, and T. Yoshimoto
Dipeptidyl Aminopeptidase IV from Stenotrophomonas maltophilia Exhibits Activity against a Substrate Containing a 4-Hydroxyproline Residue
J. Bacteriol., December 1, 2008; 190(23): 7819 - 7829.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Lorey, J. Faust, C. Mrestani-Klaus, T. Kahne, S. Ansorge, K. Neubert, and F. Buhling
Transcellular Proteolysis Demonstrated by Novel Cell Surface-associated Substrates of Dipeptidyl Peptidase IV (CD26)
J. Biol. Chem., August 30, 2002; 277(36): 33170 - 33177.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
J. M. Goldstein, A. Banbula, T. Kordula, J. A. Mayo, and J. Travis
Novel Extracellular x-Prolyl Dipeptidyl-Peptidase (DPP) from Streptococcus gordonii FSS2: an Emerging Subfamily of Viridans Streptococcal x-Prolyl DPPs
Infect. Immun., September 1, 2001; 69(9): 5494 - 5501.
[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.