Adenosylmethionine decarboxylase
http://dbpedia.org/resource/Adenosylmethionine_decarboxylase an entity of type: Thing
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.
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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
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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 eithe
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Adenosylmethionine decarboxylase
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Adenosilmetionina decarbossilasi
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Adénosylméthionine décarboxylase
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adenosylmethionine decarboxylase
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AdoMet decarboxylase
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adenosylmethionine decarboxylase
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adenosylmethionine decarboxylase 1
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crystal structure of thermotoga maritima s-adenosylmethionine decarboxylase
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P17707
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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.
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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.
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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
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