2o05 | pdb_00002o05

Human spermidine synthase

spinqualitylabelsall models 2o05, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2o05 is a 2 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 1zdz. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MTA Related: 2o06, 2o07, 2o0l Gene: SRM, SPS1 (HUMAN) Activity: Spermidine synthase, with EC number 2.5.1.16 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SPEE_HUMAN] Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Spermidine synthase 3D structures

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