Skip Navigation

Journal of Biochemistry 2006 139(1):1-9; doi:10.1093/jb/mvj019
This Article
Right arrow Full Text
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 Ikeguchi, Y.
Right arrow Articles by Pegg, A. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ikeguchi, Y.
Right arrow Articles by Pegg, A. E.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Japanese Biochemical Society.

JB Minireview--Polyamines

Aminopropyltransferases: Function, Structure and Genetics

Yoshihiko Ikeguchi1, Maria C. Bewley2 and Anthony E. Pegg3,*

1 Department of Biochemistry, Faculty of Pharmaceutical Sciences, Josai University, Sakado, Saitama 350-0295; 2 Department of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey, PA 17033, USA; and 3 Department of Cellular and Molecular Physiology, Pennsylvania State University College of Medicine, Hershey, PA 17033, USA

* To whom correspondence should be addressed. Tel: +1-717-531-8152, Fax: +1-717-531-5157, E-mail: aep1{at}psu.edu

Aminopropyltransferases use decarboxylated S-adenosylmethionine as an aminopropyl donor and an amine acceptor to form polyamines. This review covers their structure, mechanism of action, inhibition, regulation and function. The best known aminopropyltransferases are spermidine synthase and spermine synthase but other members of this family including an N1-aminopropylagmatine synthase have been characterized. Spermidine synthase is an essential gene in eukaryotes and is very widely distributed. Key regions in the active site, which are very highly conserved, were identified by structural studies with spermidine synthase from Thermotoga maritima bound to S-adenosyl-1,8-diamino-3-thiooctane, a multisubstrate analog inhibitor. A general mechanism for catalysis by aminopropyltransferases can be proposed based on these studies. Spermine synthase is less widely distributed and is not essential for growth in yeast. However, Gy mice lacking spermine synthase have multiple symptoms including a profound growth retardation, sterility, deafness, neurological abnormalities and a propensity to sudden death, which can all be prevented by transgenic expression of spermine synthase. A large reduction in spermine synthase in human males due to a splice site variant causes Snyder-Robinson syndrome with mental retardation, hypotonia and skeletal abnormalities.


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
Mol Biol EvolHome page
E. G. Minguet, F. Vera-Sirera, A. Marina, J. Carbonell, and M. A. Blazquez
Evolutionary Diversification in Polyamine Biosynthesis
Mol. Biol. Evol., October 1, 2008; 25(10): 2119 - 2128.
[Abstract] [Full Text] [PDF]


Home page
J. Med. Genet.Home page
G de Alencastro, D E McCloskey, S E Kliemann, C M C Maranduba, A E Pegg, X Wang, D R Bertola, C E Schwartz, M R Passos-Bueno, and A L Sertie
New SMS mutation leads to a striking reduction in spermine synthase protein function and a severe form of Snyder-Robinson X-linked recessive mental retardation syndrome
J. Med. Genet., August 1, 2008; 45(8): 539 - 543.
[Abstract] [Full Text] [PDF]


Home page
DevelopmentHome page
L. Muniz, E. G. Minguet, S. K. Singh, E. Pesquet, F. Vera-Sirera, C. L. Moreau-Courtois, J. Carbonell, M. A. Blazquez, and H. Tuominen
ACAULIS5 controls Arabidopsis xylem specification through the prevention of premature cell death
Development, August 1, 2008; 135(15): 2573 - 2582.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
H. Wu, J. Min, H. Zeng, D. E. McCloskey, Y. Ikeguchi, P. Loppnau, A. J. Michael, A. E. Pegg, and A. N. Plotnikov
Crystal Structure of Human Spermine Synthase: IMPLICATIONS OF SUBSTRATE BINDING AND CATALYTIC MECHANISM
J. Biol. Chem., June 6, 2008; 283(23): 16135 - 16146.
[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.