S-Adenosyl methionine <=> Decarboxylated-Adenosyl methionine + CO2

Stable Identifier
R-HSA-351222
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
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S-Adenosylmethionine decarboxylase belongs to a small class of amino acid decarboxylases that use a covalently bound pyruvate as a prosthetic group. It is an essential enzyme for polyamine biosynthesis and provides an important target for the design of anti-parasitic and cancer chemotherapeutic agents. It catalyzes the formation of the aminopropyl group donor in the biosynthesis of the polyamines spermidine and spermine. These pyruvoyl-dependent decarboxylases also form amines such as histamine, decarboxylated S-adenosylmethionine, phosphatidylethanolamine (a component of membrane phospholipids), and -alanine (a precursor of coenzyme A), which are all of critical importance in cellular physiology and provide important targets for drug design.

Literature References
PubMed ID Title Journal Year
11583147 The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase

Tolbert, WD, Ekstrom, JL, Mathews, II, Secrist JA, 3rd, Kapoor, P, Pegg, AE, Ealick, SE

Biochemistry 2001
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
adenosylmethionine decarboxylase activity of AMD1(1-67) [cytosol]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed