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- The enzyme adenosylmethionine decarboxylase (EC 4.1.1.50) catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine.Polyamines such as spermidine and spermine are essential for cellular growth under most conditions, being implicated in many cellular processes including DNA, RNA and protein synthesis. S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein. Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. These proteins can be divided into two main groups which show little sequence similarity either to each other, or to other pyruvoyl-dependent amino acid decarboxylases: class I enzymes found in bacteria and archaea, and class II enzymes found in eukaryotes. In both groups the active enzyme is generated by the post-translational autocatalytic cleavage of a precursor protein. This cleavage generates the pyruvate precursor from an internal serine residue and results in the formation of two non-identical subunits termed alpha and beta which form the active enzyme. (en)
- L'adénosylméthionine décarboxylase est une lyase qui catalyse la réaction : S-adénosyl-L-méthionine S-adénosylméthioninamine + CO2. Cette enzyme intervient dans la biosynthèse de polyamines naturelles telles que la spermidine et la spermine. Elle a pour cofacteur le pyruvate et non le phosphate de pyridoxal. (fr)
- La adenosilmetionina decarbossilasi è un enzima numero EC 4.1.1.50 appartenente alla classe delle liasi, che catalizza la seguente reazione di decarbossilazione: S-adenosil-L-metionina + H+ ⇄ S-adenosil-metioninammina + CO2 (it)
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- 3336 (xsd:nonNegativeInteger)
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- crystal structure of thermotoga maritima s-adenosylmethionine decarboxylase (en)
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- AdoMet decarboxylase (en)
- adenosylmethionine decarboxylase (en)
- adenosylmethionine decarboxylase 1 (en)
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- L'adénosylméthionine décarboxylase est une lyase qui catalyse la réaction : S-adénosyl-L-méthionine S-adénosylméthioninamine + CO2. Cette enzyme intervient dans la biosynthèse de polyamines naturelles telles que la spermidine et la spermine. Elle a pour cofacteur le pyruvate et non le phosphate de pyridoxal. (fr)
- La adenosilmetionina decarbossilasi è un enzima numero EC 4.1.1.50 appartenente alla classe delle liasi, che catalizza la seguente reazione di decarbossilazione: S-adenosil-L-metionina + H+ ⇄ S-adenosil-metioninammina + CO2 (it)
- The enzyme adenosylmethionine decarboxylase (EC 4.1.1.50) catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine.Polyamines such as spermidine and spermine are essential for cellular growth under most conditions, being implicated in many cellular processes including DNA, RNA and protein synthesis. S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein. Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. These proteins can be divided into two main groups which show little sequence similarity eithe (en)
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- Adenosylmethionine decarboxylase (en)
- Adenosilmetionina decarbossilasi (it)
- Adénosylméthionine décarboxylase (fr)
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- adenosylmethionine decarboxylase (en)
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