TY - JOUR
T1 - Spermine synthase
AU - Pegg, Anthony E.
AU - Michael, Anthony J.
N1 - Funding Information:
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.).
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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U2 - 10.1007/s00018-009-0165-5
DO - 10.1007/s00018-009-0165-5
M3 - Review article
C2 - 19859664
AN - SCOPUS:73749083095
SN - 1420-682X
VL - 67
SP - 113
EP - 121
JO - Cellular and Molecular Life Sciences
JF - Cellular and Molecular Life Sciences
IS - 1
ER -