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PROSITE documentation PDOC01038 [for PROSITE entry PS01336]

S-adenosylmethionine decarboxylase signature





Description

S-adenosylmethionine decarboxylase (EC 4.1.1.50) (AdoMetDC) [1] catalyzes the removal of the carboxylate group of S-adenosylmethionine to form S-adenosyl-5'-3-methylpropylamine which then acts as the n-propylamine group donor in the synthesis of the polyamines spermidine and spermine from putrescine.

The catalytic mechanism of AdoMetDC involves a covalently-bound pyruvoyl group. This group is post-translationally generated by a self-catalyzed intramolecular proteolytic cleavage reaction between a glutamate and a serine. This cleavage generates two chains, β (N-terminal) and α (C-terminal). The N-terminal serine residue of the α chain is then converted by nonhydrolytic serinolysis into a pyruvyol group.

As a signature pattern for AdoMetDC we selected the region that contains the proteolytic celavage site.

Note:

The AdoMetDC enzyme from Escherichia coli does not belong to this family.

Last update:

July 1999 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

ADOMETDC, PS01336; S-adenosylmethionine decarboxylase signature  (PATTERN)


Reference

1AuthorsEkstrom J.L. Mathews I.I. Stanley B.A. Pegg A.E. Ealick S.E.
TitleThe crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold.
SourceStructure 7:583-595(1999).
PubMed ID10378277



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