5-methyltetrahydrofolate-homocysteine methyltransferase - определение. Что такое 5-methyltetrahydrofolate-homocysteine methyltransferase
Diclib.com
Словарь ChatGPT
Введите слово или словосочетание на любом языке 👆
Язык:

Перевод и анализ слов искусственным интеллектом ChatGPT

На этой странице Вы можете получить подробный анализ слова или словосочетания, произведенный с помощью лучшей на сегодняшний день технологии искусственного интеллекта:

  • как употребляется слово
  • частота употребления
  • используется оно чаще в устной или письменной речи
  • варианты перевода слова
  • примеры употребления (несколько фраз с переводом)
  • этимология

Что (кто) такое 5-methyltetrahydrofolate-homocysteine methyltransferase - определение

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)

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).
5-Methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase         
CLASS OF ENZYMES
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase; EC 2.1.1.14; 5-methyltetrahydropteroyltri-L-glutamate:L-homocysteine S-methyltransferase; 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase; Tetrahydropteroyltriglutamate methyltransferase; Methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase
In enzymology, a 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
Thetin—homocysteine S-methyltransferase         
CLASS OF ENZYMES
Thetin--homocysteine S-methyltransferase; Thetin-homocysteine S-methyltransferase; EC 2.1.1.3; Dimethylsulfonioacetic acid:L-homocysteine S-methyltransferase; Dimethylthetin-homocysteine methyltransferase; Thetin-homocysteine methylpherase; Dimethylsulfonioacetate:L-homocysteine S-methyltransferase
In enzymology, a thetin-homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction

Википедия

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.