{PDOC01038}
{PS01336; ADOMETDC}
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* S-adenosylmethionine decarboxylase signature *
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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, beta (N-terminal) and alpha (C-terminal).
The N-terminal  serine  residue  of  the  alpha  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.

-Consensus pattern: [SA]-[FY]-[LIV]-L-[STN]-E-S-S-[LIVMF]-F-[LIV]
                    [The first S is the pyruvoyl forming residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

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

-Last update: July 1999 / First entry.

[ 1] Ekstrom J.L., Mathews I.I., Stanley B.A., Pegg A.E., Ealick S.E.
     "The crystal structure of human S-adenosylmethionine decarboxylase at
     2.25 A resolution reveals a novel fold."
     Structure 7:583-595(1999).
     PubMed=10378277

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