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Details on Person S-Adenosylmethionine decarboxylase belongs to a small class ...

Class:IdSummation:353574
_displayNameS-Adenosylmethionine decarboxylase belongs to a small class ...
_timestamp2008-06-12 17:23:54
created[InstanceEdit:353581] Gopinathrao, G, 2008-06-12 17:22:59
literatureReference[LiteratureReference:353589] The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase
[LiteratureReference:353533] Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase
modified[InstanceEdit:353591] Gopinathrao, G, 2008-06-12 17:23:44
textS-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.
(summation)[Reaction:351222] S-Adenosyl methionine <=> Decarboxylated-Adenosyl methionine + CO2 [Homo sapiens]
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