Abstract
Spermine is present in many organisms including animals, plants, some fungi, some archaea, and some bacteria. It is synthesized by spermine synthase, a highly specific aminopropyltransferase. This review describes spermine synthase structure, genetics, and function. Structural and biochemical studies reveal that human spermine synthase is an obligate dimer. Each monomer contains a C-terminal domain where the active site is located, a central linking domain that also forms the lid of the catalytic domain, and an N-terminal domain that is structurally very similar to S-adenosylmethionine decarboxylase. Gyro mice, which have an X-chromosomal deletion including the spermine synthase (SMS) gene, lack all spermine and have a greatly reduced size, sterility, deafness, neurological abnormalities, and a tendency to sudden death. Mutations in the human SMS lead to a rise in spermidine and reduction of spermine causing Snyder-Robinson syndrome, an X-linked recessive condition characterized by mental retardation, skeletal defects, hypotonia, and movement disorders.
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Acknowledgments
This work was supported by grants CA-018138 and GM-26290 from the National Institutes of Health, USA (to A.E.P.) and an Institute Development Fellowship (BB/E024467/1) from the Biotechnology and Biological Sciences Research Council, UK (to A.J.M.).
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Pegg, A.E., Michael, A.J. Spermine synthase. Cell. Mol. Life Sci. 67, 113–121 (2010). https://doi.org/10.1007/s00018-009-0165-5
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DOI: https://doi.org/10.1007/s00018-009-0165-5