5-methyltetrahydrofolate-homocysteine methyltransferase - traducción al Inglés
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5-methyltetrahydrofolate-homocysteine methyltransferase - traducción al Inglés

MAMMALIAN PROTEIN FOUND IN HOMO SAPIENS
5-methyltetrahydrofolate-homocysteine methyltransferase; 5-methyltetrahydrofolate-homocysteine s-methyltransferase; Homocysteine methyltransferase; Tetrahydrofolate-methyltransferase; 5-Methyltetrahydrofolate-homocysteine methyltransferase; Homocysteine-methionine methyltransferase; MTR (gene); EC 2.1.1.13; 5-methyltetrahydrofolate:L-homocysteine S-methyltransferase
  •  Homocysteine Binding Domain in Methionine Synthase. His 618, Cys 620, and Cys704 bind Zn(purple) which binds to Homocysteine(Red)
  • Methionine synthase is enzyme 4
  • Scavenger Pathway of Methionine Synthase Reductase to Recover Inactivated Methionine Synthase
  • The reaction catalyzed by methionine synthase (click to enlarge)

5-methyltetrahydrofolate-homocysteine methyltransferase         
ناقِلَةُ ميثيل الـ 5 - ميثيل تِتْراهيدْروفولات للهُوموسِيسْتئين [إنزيم]
homocysteine         
  • Total plasma homocysteine
GROUP OF STEREOISOMERS
Elevated homocysteine; Homosistine; Homocysteinemia
‎ هوموسيستئين‎
homocysteine         
  • Total plasma homocysteine
GROUP OF STEREOISOMERS
Elevated homocysteine; Homosistine; Homocysteinemia
هوموسيستئين

Definición

homocysteine
[?h?m?(?)'s?sti:n, ?h??m-, -t?i:n]
¦ noun Biochemistry an amino acid produced as an intermediate in the metabolism of methionine and cysteine.

Wikipedia

Methionine synthase

Methionine synthase also known as MS, MeSe, MTR is responsible for the regeneration of methionine from homocysteine. In humans it is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase). Methionine synthase forms part of the S-adenosylmethionine (SAMe) biosynthesis and regeneration cycle, and is the enzyme responsible for linking the cycle to one-carbon metabolism via the folate cycle. There are two primary forms of this enzyme, the Vitamin B12 (cobalamin)-dependent (MetH) and independent (MetE) forms, although minimal core methionine synthases that do not fit cleanly into either category have also been described in some anaerobic bacteria. The two dominant forms of the enzymes appear to be evolutionary independent and rely on considerably different chemical mechanisms. Mammals and other higher eukaryotes express only the cobalamin-dependent form. In contrast, the distribution of the two forms in Archaeplastida (plants and algae) is more complex. Plants exclusively possess the cobalamin-independent form, while algae have either one of the two, depending on species. Many different microorganisms express both the cobalamin-dependent and cobalamin-independent forms.