Molecular cloning of a cDNA encoding human spermine synthase.

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 Biol

journal_title

DNA and cell biology

authors

Korhonen VP,Halmekytö M,Kauppinen L,Myöhänen S,Wahlfors J,Keinänen T,Hyvönen T,Alhonen L,Eloranta T,Jänne J

doi

10.1089/dna.1995.14.841

subject

Has Abstract

pub_date

1995-10-01 00:00:00

pages

841-7

issue

10

eissn

1044-5498

issn

1557-7430

journal_volume

14

pub_type

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