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 language | English (US) |
|---|---|
| Pages (from-to) | 113-121 |
| Number of pages | 9 |
| Journal | Cellular and Molecular Life Sciences |
| Volume | 67 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2010 |
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Keywords
- Aminopropyltransferase
- Polyamines
- S-adenosylmethionine
- Spermidine
- Spermine
ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
- Molecular Medicine
- Pharmacology
- Cellular and Molecular Neuroscience
Cite this
Spermine synthase. / Pegg, Anthony E.; Michael, Anthony J.
In: Cellular and Molecular Life Sciences, Vol. 67, No. 1, 01.2010, p. 113-121.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Spermine synthase
AU - Pegg, Anthony E.
AU - Michael, Anthony J.
PY - 2010/1
Y1 - 2010/1
N2 - 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.
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.
KW - Aminopropyltransferase
KW - Polyamines
KW - S-adenosylmethionine
KW - Spermidine
KW - Spermine
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UR - http://www.scopus.com/inward/citedby.url?scp=73749083095&partnerID=8YFLogxK
U2 - 10.1007/s00018-009-0165-5
DO - 10.1007/s00018-009-0165-5
M3 - Article
C2 - 19859664
AN - SCOPUS:73749083095
VL - 67
SP - 113
EP - 121
JO - Cellular and Molecular Life Sciences
JF - Cellular and Molecular Life Sciences
SN - 1420-682X
IS - 1
ER -