Reactome | S-Adenosylmethionine decarboxylase belongs to a small class ...

Schema > Summation > Entries

created	[InstanceEdit:353581] Gopinathrao, G, 2008-06-12 17:22:59
dbId	353574
displayName	S-Adenosylmethionine decarboxylase belongs to a small class ...
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
schemaClass	Summation
text	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.

(summation)

Cite Us!