Aminopropyltransferases

Function, structure and genetics

Yoshihiko Ikeguchi, Maria Bewley, Anthony Pegg

Research output: Contribution to journalShort survey

80 Citations (Scopus)

Abstract

Aminopropyltransferases use decarboxylated S-adenosylmethionine as an aminopropyl donor and an amine acceptor to form polyamines. This review covers their structure, mechanism of action, inhibition, regulation and function. The best known aminopropyl-transferases are spermidine synthase and spermine synthase but other members of this family including an N 1- aminopropylagmatine synthase have been characterized. Spermidine synthase is an essential gene in eukaryotes and is very widely distributed. Key regions in the active site, which are very highly conserved, were identified by structural studies with spermidine synthase from Thermotoga maritima bound to S-adenosyl-1,8-diamino-3-thiooctane, a multisubstrate analog inhibitor. A general mechanism for catalysis by aminopropyltransferases can be proposed based on these studies. Spermine synthase is less widely distributed and is not essential for growth in yeast. However, Gy mice lacking spermine synthase have multiple symptoms including a profound growth retardation, sterility, deafness, neurological abnormalities and a propensity to sudden death, which can all be prevented by transgenic expression of spermine synthase. A large reduction in spermine synthase in human males due to a splice site variant causes Snyder-Robinson syndrome with mental retardation, hypotonia and skeletal abnormalities.

Original languageEnglish (US)
Pages (from-to)1-9
Number of pages9
JournalJournal of Biochemistry
Volume139
Issue number1
DOIs
StatePublished - Jan 1 2006

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Spermine Synthase
Spermidine Synthase
Genetic Structures
Thermotoga maritima
Muscle Hypotonia
Essential Genes
Polyamines
Deafness
Growth
Transferases
Sudden Death
Eukaryota
Catalysis
Yeast
Infertility
Amines
Catalytic Domain
Genes
Yeasts
Genetics

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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title = "Aminopropyltransferases: Function, structure and genetics",
abstract = "Aminopropyltransferases use decarboxylated S-adenosylmethionine as an aminopropyl donor and an amine acceptor to form polyamines. This review covers their structure, mechanism of action, inhibition, regulation and function. The best known aminopropyl-transferases are spermidine synthase and spermine synthase but other members of this family including an N 1- aminopropylagmatine synthase have been characterized. Spermidine synthase is an essential gene in eukaryotes and is very widely distributed. Key regions in the active site, which are very highly conserved, were identified by structural studies with spermidine synthase from Thermotoga maritima bound to S-adenosyl-1,8-diamino-3-thiooctane, a multisubstrate analog inhibitor. A general mechanism for catalysis by aminopropyltransferases can be proposed based on these studies. Spermine synthase is less widely distributed and is not essential for growth in yeast. However, Gy mice lacking spermine synthase have multiple symptoms including a profound growth retardation, sterility, deafness, neurological abnormalities and a propensity to sudden death, which can all be prevented by transgenic expression of spermine synthase. A large reduction in spermine synthase in human males due to a splice site variant causes Snyder-Robinson syndrome with mental retardation, hypotonia and skeletal abnormalities.",
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Aminopropyltransferases : Function, structure and genetics. / Ikeguchi, Yoshihiko; Bewley, Maria; Pegg, Anthony.

In: Journal of Biochemistry, Vol. 139, No. 1, 01.01.2006, p. 1-9.

Research output: Contribution to journalShort survey

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AU - Pegg, Anthony

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