Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references
Chemical compound
Methionine (symbol Met or M)[3] (/mɪˈθaɪəniːn/)[4] is an essential amino acid in humans.
As the precursor of other non-essential amino acids such as cysteine and taurine, versatile compounds such as SAM-e, and the important antioxidant glutathione, methionine plays a critical role in the metabolism and health of many species, including humans. Methionine is also involved in angiogenesis and various processes related to DNA transcription, epigenetic expression, and gene regulation.
Methionine was first isolated in 1921 by John Howard Mueller.[5] It is encoded by the codon AUG. It was named by Satoru Odake in 1925, as an abbreviation of its structural description 2-amino-4-(methylthio)butanoic acid.[6]
^Dawson RM, Elliott DC, Elliott WH, Jones KM (1959). Data for Biochemical Research. Oxford: Clarendon Press.
^Weast, Robert C., ed. (1981). CRC Handbook of Chemistry and Physics (62nd ed.). Boca Raton, FL: CRC Press. p. C-374. ISBN 0-8493-0462-8..
^"Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Archived from the original on 9 October 2008. Retrieved 5 March 2018.
^"Methionine". Oxford University Press. Archived from the original on January 27, 2018.
^Pappenheimer AM (1987). "A Biographical Memoir of John Howard Mueller" (PDF). Washington D.C.: National Academy of Sciences.
^Odake, Satoru (1925). "On the Occurrence of a Sulphur-containing Amino acid in Yeast". Bulletin of the Agricultural Chemical Society of Japan. 1 (8): 87–89. doi:10.1271/bbb1924.1.87. ISSN 1881-1272.
Methionine (symbol Met or M) (/mɪˈθaɪəniːn/) is an essential amino acid in humans. As the precursor of other non-essential amino acids such as cysteine...
Oxidation of the sulfur of methionine results in methionine sulfoxide or methionine sulfone. The sulfur-containing amino acids methionine and cysteine are more...
Methionine synthase (MS, MeSe, MTR) is primarily responsible for the regeneration of methionine from homocysteine in most individuals. In humans it is...
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Methionine transaminase (EC 2.6.1.88, methionine-oxo-acid transaminase) is an enzyme with systematic name L-methionine:2-oxo-acid aminotransferase. This...
biosynthesized from methionine by the removal of its terminal Cε methyl group. In the body, homocysteine can be recycled into methionine or converted into...
a methionine racemase (EC 5.1.1.2) is an enzyme that catalyzes the chemical reaction L-methionine ⇌ {\displaystyle \rightleftharpoons } D-methionine Hence...
Methionine sulfoxide reductase may refer to: Methionine-S-oxide reductase L-methionine (S)-S-oxide reductase This set index page lists enzyme articles...
Methionyl aminopeptidase (EC 3.4.11.18, methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP) is an enzyme. This enzyme catalyses the...
by solvent evaporation; they belong to the triclinic space group P1. L-methionine L-methioninium hydrogen maleate also belongs to the amino acid family...
of the metabolism of the amino acid methionine due to a deficiency of cystathionine beta synthase or methionine synthase. It is an inherited autosomal...
variations of the disease, these being those presenting methionine homozygotes at codon 129 and methionine/valine heterozygotes being the most severe in the...
N-methylhistidine, and two isomers of N-methylarginine. Methionine synthase regenerates methionine (Met) from homocysteine (Hcy). The overall reaction transforms...
10-methylenetetrahydrofolate (MTHF) and used to recycle homocysteine back to methionine by methionine synthase (MS). L-Methylfolate is water-soluble and primarily excreted...
Hypermethioninemia is an excess of the amino acid methionine, in the blood. This condition can occur when methionine is not broken down properly in the body. Hypermethioninemia...
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