5-Methyltetrahydrofolate-homocysteine methyltransferase
(Redirected from Tetrahydrofolate-methyltransferase)
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5-methyltetrahydrofolate-homocysteine methyltransferase | |
---|---|
Identifiers | |
Symbol | MTR |
Entrez | 4548 |
HUGO | 7468 |
OMIM | 156570 |
RefSeq | NM_000254 |
UniProt | Q99707 |
Other data | |
EC number | 2.1.1.13 |
Locus | Chr. 1 q43 |
5-Methyltetrahydrofolate-homocysteine methyltransferase or (MTR) is an enzyme responsible for the production of methionine from homocysteine. MTR forms part of the S-adenosyl methionine cycle and is also called methionine synthase.[1]
Function
MTR contains the cofactor - methylcobalamin (MeB12) and uses the substrates N5-methyl-tetrahydrofolate (N5-methyl-THF) and homocysteine.
The enzyme works in two steps in a ping-pong reaction. First, methylcobalamin is formed by a methyl group transfer from N5-mTHF with formation of MeB12 and tetrahydrofolate (THF). In the second step, MeB12 transfers this methyl group to (homocysteine), regenerating the cofactor cobalamin and releasing the product methionine
File:VitaminB12 2.png
The MTR reaction
See also
References
- ↑ Banerjee RV, Matthews RG (1990). "Cobalamin-dependent methionine synthase" (PDF). FASEB J. 4 (5): 1450–9. PMID 2407589.
External links
- ENZYME: EC 2.1.1.13
- 5-Methyltetrahydrofolate-Homocysteine+S-Methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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