2O06

Human spermidine synthase

Summary for 2O06

• Entry DOI: 10.2210/pdb2o06/pdb
• Related: 2O05 2O07 2O0L
• Descriptor: Spermidine synthase, MAGNESIUM ION, 5'-DEOXY-5'-METHYLTHIOADENOSINE, ... (5 entities in total)
• Functional Keywords: spermidine synthase, structural genomics, structural genomics consortium, sgc, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 68847.38

Authors

Min, J.,Wu, H.,Zeng, H.,Loppnau, P.,Weigelt, J.,Sundstrom, M.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Plotnikov, A.N.,Structural Genomics Consortium (SGC) (deposition date: 2006-11-27, release date: 2006-12-12, Last modification date: 2023-12-27)

Primary citation

Wu, H.,Min, J.,Ikeguchi, Y.,Zeng, H.,Dong, A.,Loppnau, P.,Pegg, A.E.,Plotnikov, A.N.
Structure and mechanism of spermidine synthases.
Biochemistry, 46:8331-8339, 2007

PubMed Abstract: 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.

PubMed: 17585781
DOI: 10.1021/bi602498k

Experimental method

X-RAY DIFFRACTION (2 Å)