5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
"5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
An enzyme that catalyzes the formation of methionine by transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine. It requires a cobamide coenzyme. The enzyme can act on mono- or triglutamate derivatives. EC 2.1.1.13.
| Descriptor ID |
D013766
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| MeSH Number(s) |
D08.811.913.555.500.645
|
| Concept/Terms |
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase- 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
- S-Methyltransferase, 5-Methyltetrahydrofolate-Homocysteine
- Methyltetrahydrofolate Homocysteine Methyltransferase
- Homocysteine Methyltransferase, Methyltetrahydrofolate
- Methyltransferase, Methyltetrahydrofolate Homocysteine
- Methionine Synthase
- Synthase, Methionine
- Methionine Synthetase
- Synthetase, Methionine
- Tetrahydropteroylglutamate Methyltransferase
- Methyltransferase, Tetrahydropteroylglutamate
|
Below are MeSH descriptors whose meaning is more general than "5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase".
Below are MeSH descriptors whose meaning is more specific than "5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase".
This graph shows the total number of publications written about "5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase" by people in this website by year, and whether "5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 1 | 0 | 1 |
| 2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase" by people in Profiles.
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Altered Methionine Metabolism in Cancer Cells. Methods Mol Biol. 2019; 1866:13-26.
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Molecular basis for dysfunction of some mutant forms of methylmalonyl-CoA mutase: deductions from the structure of methionine synthase. Proc Natl Acad Sci U S A. 1996 May 28; 93(11):5550-5.
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Cobalamin coenzyme synthesis in normal and mutant human fibroblasts. Evidence for a processing enzyme activity deficient in cblC cells. J Biol Chem. 1979 Dec 10; 254(23):11847-53.
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Cobalamin binding and cobalamin-dependent enzyme activity in normal and mutant human fibroblasts. J Clin Invest. 1978 Nov; 62(5):952-60.
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Intracellular binding of radioactive hydroxocobalamin to cobalamin-dependent apoenzymes in rat liver. Proc Natl Acad Sci U S A. 1977 Mar; 74(3):916-20.