Structure and Mechanism of Spermidine Synthases

Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors, forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase, which is highly specific for putrescine as the amine acceptor, and the The...

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Bibliographic Details
Published in:Biochemistry (Easton) 2007-07, Vol.46 (28), p.8331-8339
Main Authors: Wu, Hong, Min, Jinrong, Ikeguchi, Yoshihiko, Zeng, Hong, Dong, Aiping, Loppnau, Peter, Pegg, Anthony E, Plotnikov, Alexander N
Format: Article
Language:English
Subjects:
Binding Sites
Crystallography, X-Ray
Humans
Models, Molecular
Mutagenesis, Site-Directed
Putrescine - chemistry
Spermidine Synthase - chemistry
Spermidine Synthase - genetics
Substrate Specificity
Thermotoga maritima - enzymology
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Summary:Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors, forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase, which is highly specific for putrescine as the amine acceptor, and the Thermotoga maritima spermidine synthase, which prefers putrescine but is more tolerant of other substrates. Comparison of the structures of the human spermidine synthase with both substrates and products with the known structure of T. maritima spermidine synthase complexed to a multisubstrate analogue inhibitor and analysis of the properties of site-directed mutants provide a general mechanistic hypothesis for the aminopropyl transfer reaction. The studies also provide a structural basis for the specificity of the spermidine synthase subclass of the aminopropyltransferase family.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi602498k