S-adenosyl-L-methionine decarboxylase - vertaling naar Engels
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S-adenosyl-L-methionine decarboxylase - vertaling naar Engels

CLASS OF ENZYMES
S-adenosylmethionine decarboxylase; EC 4.1.1.50; S-adenozil-L-metionin carboxy-lyase ((5-deoxy-5-adenozil)(3-aminopropyl)methylsulfonium-salt-forming)

S-adenosyl-L-methionine decarboxylase      

медицина

S-аденозил-L-метиониндекарбоксилаза

S-adenosylhomocysteine         
CHEMICAL COMPOUND
S-Adenosyl-L-Homocisteine; S-adenosyl-L-homocysteine; S-adenosylhomocysteine; S-adenosyl homocysteine; 2-S-adenosyl-L-homocysteine; AdoHcy; C14H20N6O5S; S-Adenosylhomocysteine

медицина

аденозилгомоцистеин-S

adenosylmethionine         
  • S<sub>N</sub>2]]-like methyl transfer reaction. Only the SAM cofactor and cytosine base are shown for simplicity.
CHEMICAL COMPOUND FOUND IN ALL DOMAINS OF LIFE WITH LARGELY UNEXPLORED EFFECTS
SAM-e; S-adenosyl-methionine; Sam-e; S-adenosylmethionine; SAMe; S-adenosyl methionine; S-Adenosylmethionine; S-Adenosyl-L-methionine; S-adenosyl-L-methionine; Ademetionine; S-adenosyl-l-methionine; Same-E; Adomet; S-adenosylmethione; C15H22N6O5S+; C15H22N6O5S; ATC code A16AA02; ATCvet code QA16AA02; SAMe Rx-Mood; Sam-Sulfate; EC 2.4.2.13; SAM cofactor; Radical-SAM; Adenosylmethionine; AdoMet

медицина

аденозилметионин

Definitie

L-формы бактерий

Wikipedia

Adenosylmethionine decarboxylase

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.

Vertaling van &#39S-adenosyl-L-methionine decarboxylase&#39 naar Russisch