Spermine synthase |
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Authors: | Anthony E Pegg Anthony J Michael |
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Institution: | (1) Department of Cellular and Molecular Physiology, Milton S. Hershey Medical Center, Pennsylvania State University College of Medicine, Hershey, PA 17033, USA;(2) Institute of Food Research, Norwich, NR4 7UA, UK |
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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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Keywords: | |
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