Methionine

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Methionine
IUPAC name	Methionine
Other names	2-amino-4-(methylthio)butanoic acid
Identifiers
Abbreviations	Met, M
CAS number	59-51-8 Y, 63-68-3 (L-isomer) 348-67-4 (D-isomer)
PubChem	876
EC-number	200-432-1
ATC code	V03AB26,QA05BA90, QG04BA90
SMILES	CSCC[C@H](N)C(O)=O
InChI	1/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)
ChemSpider ID	853
Properties[1]
Molecular formula	C5H11NO2S
Molar mass	149.21 g mol−1
Appearance	white crystalline powder
Density	1.340 g/cm3
Melting point	281 ºC decomp.
Solubility in water	soluble
Supplementary data page
Structure and properties	n, εr, etc.
Thermodynamic data	Phase behaviour Solid, liquid, gas
Spectral data	UV, IR, NMR, MS
Y (what is this?) (verify) Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Infobox references

Methionine (pronounced /mɛˈθaɪ.ɵniːn, mɛˈθaɪ.ɵnɪn/; abbreviated as Met or M)^[2] is an α-amino acid with the chemical formula HO₂CCH(NH₂)CH₂CH₂SCH₃. This essential amino acid is classified as nonpolar.

Contents 1 Function 2 Betaines 3 Biosynthesis 4 Other biochemical pathways 4.1 Generation of homocysteine 4.2 Regeneration of methionine 4.3 Conversion to cysteine 5 Synthesis 6 Dietary aspects 7 See also 8 References 9 External links

[edit] Function

Together with cysteine, methionine is one of two sulfur-containing proteinogenic amino acids. Its derivative S-adenosyl methionine (SAM) serves as a methyl donor. Methionine is an intermediate in the biosynthesis of cysteine, carnitine, taurine, lecithin, phosphatidylcholine, and other phospholipids. Improper conversion of methionine can lead to atherosclerosis.

This amino acid is also used by plants for synthesis of ethylene. The process is known as the Yang Cycle or the methionine cycle.

Methionine is one of only two amino acids encoded by a single codon (AUG) in the standard genetic code (tryptophan, encoded by UGG, is the other). The codon AUG is also the "Start" message for a ribosome that signals the initiation of protein translation from mRNA. As a consequence, methionine is incorporated into the N-terminal position of all proteins in eukaryotes and archaea during translation, although it is usually removed by post-translational modification.

[edit] Betaines

(S)-Methionine (left) and (R)-methionine (right) in zwitterionic form at neutral pH

[edit] Biosynthesis

As an essential amino acid, methionine is not synthesized in humans, hence we must ingest methionine or methionine-containing proteins. In plants and microorganisms, methionine is synthesized via a pathway that uses both aspartic acid and cysteine. First, aspartic acid is converted via β-aspartyl-semialdehyde into homoserine, introducing the pair of contiguous methylene groups. Homoserine converts to O-succinyl homoserine, which then reacts with cysteine to produce cystathionine, which is cleaved to yield homocysteine. Subsequent methylation of the thiol group by folates affords methionine. Both cystathionine-γ-synthase and cystathionine-β-lyase require Pyridoxyl-5'-phosphate as a cofactor, whereas homocysteine methyltransferase requires Vitamin B12 as a cofactor.^[3]

Enzymes involved in methionine biosynthesis:

1. aspartokinase
2. β-aspartate semialdehyde dehydrogenase
3. homoserine dehydrogenase
4. homoserine acyltransferase
5. cystathionine-γ-synthase
6. cystathionine-β-lyase
7. methionine synthase (in mammals, this step is performed by homocysteine methyltransferase)

Methionine biosynthesis

[edit] Other biochemical pathways

Fates of methionine

Although mammals cannot synthesize methionine, they can still utilize it in a variety of biochemical pathways:

[edit] Generation of homocysteine

Methionine is converted to S-adenosylmethionine (SAM) by (1) methionine adenosyltransferase.

SAM serves as a methyl-donor in many (2) methyltransferase reactions and is converted to S-adenosylhomocysteine (SAH).

(3) adenosylhomocysteinase converts SAH to homocysteine.

There are two fates of homocysteine: it can be used to regenerate methionine, or to form cysteine.

[edit] Regeneration of methionine

Methionine can be regenerated from homocysteine via (4) methionine synthase.

It can also be remethylated using glycine betaine (NNN-trimethyl glycine) to methionine via the enzyme Betaine-homocysteine methyltransferase (E.C.2.1.1.5, BHMT). BHMT makes up to 1.5% of all the soluble protein of the liver, and recent evidence suggests that it may have a greater influence on methionine and homocysteine homeostasis than methionine synthase.

[edit] Conversion to cysteine

Homocysteine can be converted to cysteine.

• (5) Cystathionine-β-synthase (a PLP-dependent enzyme) combines homocysteine and serine to produce cystathionine. Instead of degrading cystathionine via cystathionine-β-lyase, as in the biosynthetic pathway, cystathionine is broken down to cysteine and α-ketobutyrate via (6) cystathionine-γ-lyase.
• (7) α-ketoacid dehydrogenase converts α-ketobutyrate to propionyl-CoA, which is metabolized to succinyl-CoA in a three-step process (see propionyl-CoA for pathway).

[edit] Synthesis

Racemic methionine can be synthesized from diethyl sodium phthalimidomalonate by alkylation with chloroethylmethylsulfide (ClCH₂CH₂SCH₃) followed by hydrolysis and decarboxylation.^[4]

[edit] Dietary aspects

High levels of methionine can be found in sesame seeds, Brazil nuts, fish, meats and some other plant seeds. Most fruits and vegetables contain very little of it. Most legumes are also low in methionine.

Racemic methionine is sometimes added as an ingredient to pet foods.^[6]

Methionine restriction without energy restriction extends mouse lifespan.^[7]

[edit] See also

• Allantoin
• Formylmethionine
• Paracetamol_poisoning#Treatment - A Methionine-Paracetamol preparation that might prevent hepatotoxicity.
• Photo-reactive methionine

[edit] References

[edit] External links

• Foods containing methionine
• Computational Chemistry Wiki