Abstract:
:We have isolated and sequenced cDNA clones that encode human spermine synthase (EC 2.5.1.22). The total length of the sequenced cDNA was 1,612 nucleotides, containing an open reading frame encoding a polypeptide chain of 368 amino acids. All of the previously sequenced peptide fragments of human and bovine spermine synthase proteins could be located within the coding region derived from the cDNA. An unusual sequence of AATTAA apparently signaled the initiation of polyadenylation. Sequence comparisons between human spermine synthase and spermidine synthases from bacterial and mammalian sources revealed a nearly complete lack of similarity between the primary structures of these two enzymes catalyzing almost identical reactions. A modest similarity found was restricted to a relatively short peptide domain apparently involved in the binding of decarboxylated S-adenosylmethionine, the common substrate for both enzymes. The apparent lack of an overall similarity may indicate that spermine synthase, the enzyme found only in eukaryotes, and spermidine synthase with more universal distribution, although functionally closely related, have evolved separately.
journal_name
DNA Cell Bioljournal_title
DNA and cell biologyauthors
Korhonen VP,Halmekytö M,Kauppinen L,Myöhänen S,Wahlfors J,Keinänen T,Hyvönen T,Alhonen L,Eloranta T,Jänne Jdoi
10.1089/dna.1995.14.841subject
Has Abstractpub_date
1995-10-01 00:00:00pages
841-7issue
10eissn
1044-5498issn
1557-7430journal_volume
14pub_type
杂志文章abstract::FOXO3 is a member of the Forkhead box class O (FOXO) transcription factor family that modulates the transcription of target genes in a variety of cellular functions in lower animals to mammals. It has been implicated in the attenuation of insulin-signaling pathways, including having a potential role in lifespan contro...
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