Spermine synthase

Anthony Pegg, Anthony J. Michael

Research output: Contribution to journalReview article

72 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)113-121
Number of pages9
JournalCellular and Molecular Life Sciences
Volume67
Issue number1
DOIs
StatePublished - Jan 1 2010

Fingerprint

Spermine Synthase
Spermine
Catalytic Domain
Spermidine Synthase
Adenosylmethionine Decarboxylase
Muscle Hypotonia
Spermidine
Genetic Structures
Archaea
Movement Disorders
Deafness
Sudden Death
Intellectual Disability
Infertility
Fungi
Bacteria
Mutation
Genes

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

Cite this

Pegg, Anthony ; Michael, Anthony J. / Spermine synthase. In: Cellular and Molecular Life Sciences. 2010 ; Vol. 67, No. 1. pp. 113-121.
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Spermine synthase. / Pegg, Anthony; Michael, Anthony J.

In: Cellular and Molecular Life Sciences, Vol. 67, No. 1, 01.01.2010, p. 113-121.

Research output: Contribution to journalReview article

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AB - 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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