5-Methyltetrahydrofolate-homocysteine methyltransferase
(Redirected from MTR)
| 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
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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