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[Methionine synthase] reductase, or Methionine synthase reductase, [1] encoded by the gene MTRR, is an enzyme that is responsible for the reduction of methionine synthase inside human body. This enzyme is crucial for maintaining the one carbon metabolism, specifically the folate cycle .
The Methionine Synthase Reductase (MTRR) gene primarily acts in the reductive regeneration of cob(I)alamin (vitamin B12). [10] Cob(I)alamin is a cofactor that maintains activation of the methionine synthase enzyme (MTR) Methionine synthase, linking folate and methionine metabolism. Donation of methyl groups from folate are utilized for cellular ...
The reactivation domain binds SAM and is the site of interaction with flavodoxin or Methionine Synthase Reductase during the reactivation cycle of the enzyme. [ 17 ] [ 16 ] [ 20 ] The cobalamin-binding domain contains two subdomains, with the cofactor bound to the Rossman-fold B 12 -binding subdomain, which is in turn capped by the other ...
Msr is ubiquitous and highly conserved. Human and animal studies have shown the highest levels of expression in kidney and liver. It carries out the enzymatic reduction of methionine sulfoxide (MetO), the oxidized form of the amino acid methionine (Met), back to methionine, using thioredoxin to catalyze the enzymatic reduction and repair of oxidized methionine residues. [7]
Methylenetetrahydrofolate reductase (MTHFR) is the rate-limiting enzyme in the methyl cycle, and it is encoded by the MTHFR gene. [5] Methylenetetrahydrofolate reductase catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate , a cosubstrate for homocysteine remethylation to methionine .
It is the one-carbon donor for thymidylate synthase, for methylation of 2-deoxy-uridine-5-monophosphate to 2-deoxy-thymidine-5-monophosphate . The coenzyme is necessary for the biosynthesis of thymidine and is the C1-donor in the reactions catalyzed by TS and thymidylate synthase (FAD).
Levomefolic acid is generated by methylenetetrahydrofolate reductase (MTHFR) from 5,10-methylenetetrahydrofolate (MTHF) and used to recycle homocysteine back to methionine by methionine synthase (MS). [2] L-Methylfolate is water-soluble and primarily excreted via the kidneys.
Thus, the two substrates of this enzyme are 5-methyltetrahydropteroyltri-L-glutamate and L-homocysteine, whereas its two products are tetrahydropteroyltri-L-glutamate and L-methionine. This enzyme participates in methionine metabolism. It has 2 cofactors: orthophosphate, and zinc.