L-methionine
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L-methionine

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L-methionine is a non-polar α-amino acid with a straight side chain that possess a S-methyl thioether (i.e. C-S-C bonding) at the γ-carbon. It is an essential amino acid in all metazoa and is coded by the initiation codon AUG, which also indicates mRNA's coding region where translation into protein begins.
Protein supplement in health care products.

Category
L-Amino Acids
Catalog number
BAT-014309
CAS number
63-68-3
Molecular Formula
C5H11NO2S
Molecular Weight
149.20
L-methionine
IUPAC Name
(2S)-2-amino-4-methylsulfanylbutanoic acid
Synonyms
(S)-2-Amino-4-(methylthio)butanoic Acid; Cymethion; S-Methyl-L-momocysteine; L-α-Amino-γ-methylthiobutyric Acid; Methionine; NSC 22946; S-Methionine; S-Methyl-L-homocysteine; α-Amino-γ-methylmercaptobutyric Acid; γ-Methylthio-α-aminobutyric Acid; H-Met-OH
Appearance
White to Off-white Crystalline Powder
Purity
98%
Density
1.2±0.1 g/cm3
Melting Point
284°C (dec.)
Boiling Point
306.9±37.0°C at 760 mmHg
Storage
Store at 2-8°C
Solubility
Soluble in Aqueous Acid (Sparingly), DMSO (Slightly), Water (Slightly)
InChI
InChI=1S/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1
InChI Key
FFEARJCKVFRZRR-BYPYZUCNSA-N
Canonical SMILES
CSCCC(C(=O)O)N
1.The enzymatic activities of brain catechol-O-methyltransferase (COMT) and methionine sulphoxide reductase are correlated in a COMT Val/Met allele-dependent fashion.
Moskovitz J;Walss-Bass C;Cruz DA;Thompson PM;Hairston J;Bortolato M Neuropathol Appl Neurobiol. 2015 Dec;41(7):941-51. doi: 10.1111/nan.12219. Epub 2015 May 2.
AIMS: ;The enzyme catechol-O-methyltransferase (COMT) plays a primary role in the metabolism of catecholamine neurotransmitters and is implicated in the modulation of cognitive and emotional responses. The best characterized single nucleotide polymorphism (SNP) of the COMT gene consists of a valine (Val)-to-methionine (Met) substitution at codon 108/158. The Met-containing variant confers a marked reduction in COMT catalytic activity. We recently showed that the activity of recombinant COMT is positively regulated by the enzyme Met sulphoxide reductase (MSR), which counters the oxidation of Met residues of proteins. The current study was designed to assess whether brain COMT activity may be correlated to MSR in an allele-dependent fashion.;METHODS: ;COMT and MSR activities were measured from post-mortem samples of prefrontal cortices, striata and cerebella of 32 subjects by using catechol and dabsyl-Met sulphoxide as substrates, respectively. Allelic discrimination of COMT Val(108/185) Met SNP was performed using the Taqman 5'nuclease assay.;RESULTS: ;Our studies revealed that, in homozygous carriers of Met, but not Val alleles, the activity of COMT and MSR was significantly correlated throughout all tested brain regions.
2.Molecular and cellular effects of vitamin B12 in brain, myocardium and liver through its role as co-factor of methionine synthase.
Guéant JL;Caillerez-Fofou M;Battaglia-Hsu S;Alberto JM;Freund JN;Dulluc I;Adjalla C;Maury F;Merle C;Nicolas JP;Namour F;Daval JL Biochimie. 2013 May;95(5):1033-40. doi: 10.1016/j.biochi.2013.01.020. Epub 2013 Feb 14.
Vitamin B12 (cobalamin, cbl) is a cofactor of methionine synthase (MTR) in the synthesis of methionine, the precursor of the universal methyl donor S-Adenosylmethionine (SAM), which is involved in epigenomic regulatory mechanisms. We have established a neuronal cell model with stable expression of a transcobalamin-oleosin chimer and subsequent decreased cellular availability of vitamin B12, which produces reduced proliferation, increased apoptosis and accelerated differentiation through PP2A, NGF and TACE pathways. Anti-transcobalamin antibody or impaired transcobalamin receptor expression produce also impaired proliferation in other cells. Consistently, the transcription, protein expression and activity of MTR are increased in proliferating cells of skin and intestinal epitheliums, in rat intestine crypts and in proliferating CaCo2 cells, while MTR activity correlates with DNA methylation in rat intestine villi. Exposure to nitrous oxide in animal models identified impairment of MTR reaction as the most important metabolic cause of neurological manifestations of B12 deficiency. Early vitamin B12 and folate deprivation during gestation and lactation of a 'dam-progeny' rat model developed in our laboratory is associated with long-lasting disabilities of behavior and memory capacities, with persisting hallmarks related to increased apoptosis, impaired neurogenesis and altered plasticity.
3.Structural scaffold of 18-crown-6 tetracarboxylic acid for optical resolution of chiral amino acid: X-ray crystal analyses and energy calculations of complexes of D- and L-isomers of tyrosine, isoleucine, methionine and phenylglycine.
Nagata H;Nishi H;Kamigauchi M;Ishida T Org Biomol Chem. 2004 Dec 7;2(23):3470-5. Epub 2004 Oct 22.
To clarify the structural scaffold of (+)-18-crown-6 tetracarboxylic acid ((+)-18C6H4) for the optical resolution of a chiral amino acid, the crystal structures of its equimolar complexes with L- and D-isomers of tyrosine (Tyr), isoleucine (Ile), methionine (Met) and phenylglycine (PheG) were analysed by X-ray diffraction methods. (+)-18C6H4 took very similar conformations for all complexes. Although the chemical structure of (+)-18C6H4 is C2-symmetric, it took a similar asymmetric ring conformation of radius ca. 6.0 A. In all complexes, the amino group of chiral amino acids was located near the center of the ring and formed three hydrogen bonds and five electrostatic interactions with eight oxygen atoms of the ether ring and carboxyl groups. Also, the Calpha atom of chiral amino acids participated in Calpha-H...O interaction with the oxygen atom of (+)-18C6H4. In contrast, the carboxyl group of chiral amino acids did not directly interact with (+)-18C6H4. These results indicate that the structural scaffold of (+)-18C6H4 for the optical resolution of chiral amino acids is mainly based on the mode of interaction of (+)-18C6H4 with the amino and Calpha-H groups of chiral amino acids. The differences in interaction pattern and binding energy between the L- and D-isomers of each amino acid are discussed in relation to the chiral recognition of (+)-18C6H4.
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