2o05
From Proteopedia
Human spermidine synthase
Overview
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.
About this Structure
2O05 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1zdz. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of spermidine synthases., Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN, Biochemistry. 2007 Jul 17;46(28):8331-9. Epub 2007 Jun 22. PMID:17585781 Page seeded by OCA on Sun May 4 10:08:29 2008
Categories: Homo sapiens | Single protein | Spermidine synthase | Arrowsmith, C H. | Bochkarev, A. | Edwards, A M. | Loppnau, P. | Min, J. | Plotnikov, A N. | SGC, Structural Genomics Consortium. | Sundstrom, M. | Weigelt, J. | Wu, H. | Zeng, H. | Sgc | Structural genomic | Structural genomics consortium
