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Identification
YMDB IDYMDB00318
NameL-Methionine
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionMethionine (abbreviated as Met or M) is an alpha-amino acid. The L-isomer is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. It is classified as a nonpolar amino acid, because of the hydrophobic nature of the thioether-alkyl side chain. 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. 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. The principal fates methionine are incorporation into polypeptide chains, and use in the production of alpha-ketobutyrate and cysteine via SAM (S-adenosylmethionine). The transulfuration reactions that produce cysteine from homocysteine and serine also produce alpha-ketobutyrate, the latter being converted first to propionyl-CoA and then via a 3-step process to succinyl-CoA.
Structure
Thumb
Synonyms
  • (2S)-2-amino-4-(methylsulfanyl)butanoate
  • (2S)-2-amino-4-(methylsulfanyl)butanoic acid
  • (l)-methionine
  • (s)-(+)-methionine
  • (S)-2-amino-4-(methylthio)-Butanoate
  • (S)-2-amino-4-(methylthio)-Butanoic acid
  • (S)-2-Amino-4-(methylthio)butanoate
  • (S)-2-Amino-4-(methylthio)butanoic acid
  • (S)-2-amino-4-(methylthio)butyric acid
  • (s)-methionine
  • 2-Amino-4-(methylthio)butyrate
  • 2-Amino-4-(methylthio)butyric acid
  • 2-Amino-4-methylthiobutanoate
  • 2-Amino-4-methylthiobutanoic acid
  • A-amino-g-methylmercaptobutyrate
  • A-amino-g-methylmercaptobutyric acid
  • Acimethin
  • alpha-amino-alpha-aminobutyric acid
  • alpha-amino-gamma-methylmercaptobutyrate
  • Alpha-amino-gamma-methylmercaptobutyric acid
  • Cymethion
  • G-methylthio-a-aminobutyrate
  • G-methylthio-a-aminobutyric acid
  • gamma-methylthio-alpha-aminobutyrate
  • gamma-methylthio-alpha-aminobutyric acid
  • H-met-h
  • H-met-oh
  • L-(-)-methionine
  • l-2-Amino-4-(methylthio)butyric acid
  • L-2-Amino-4methylthiobutyric acid
  • L-a-amino-g-methylthiobutyrate
  • L-a-amino-g-methylthiobutyric acid
  • L-alpha-amino-gamma-methylmercaptobutyric acid
  • L-alpha-amino-gamma-methylthiobutyrate
  • L-alpha-amino-gamma-methylthiobutyric acid
  • L-gamma-methylthio-alpha-aminobutyric acid
  • L-methionin
  • L-Methionine
  • L-methioninum
  • L(-)-amino-alpha-amino-alpha-aminobutyric acid
  • L(-)-amino-gamma-methylthiobutyric acid
  • Liquimeth
  • Mepron
  • MET
  • Methilanin
  • Methionine
  • Methioninum
  • Metionina
  • Neo-methidin
  • Poly-l-methionine
  • Polymethionine
  • S-methionine
  • S-methyl-l-homocysteine
  • M
  • L-Methionine Z
  • (2S)-2-Amino-4-(methylsulphanyl)butanoate
  • (2S)-2-Amino-4-(methylsulphanyl)butanoic acid
  • (S)-2-Amino-4-(methylthio)butyrate
  • L-a-Amino-g-methylmercaptobutyrate
  • L-a-Amino-g-methylmercaptobutyric acid
  • L-alpha-Amino-gamma-methylmercaptobutyrate
  • L-Α-amino-γ-methylmercaptobutyrate
  • L-Α-amino-γ-methylmercaptobutyric acid
  • L-2-Amino-4methylthiobutyrate
  • L-2-Amino-4-methylthiobutyric acid
  • Toxin war
  • L-Isomer methionine
  • Methionine, L-isomer
  • Pedameth
  • Methionine, L isomer
CAS number63-68-3
WeightAverage: 149.211
Monoisotopic: 149.051049291
InChI KeyFFEARJCKVFRZRR-BYPYZUCNSA-N
InChIInChI=1S/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1
IUPAC Name(2S)-2-amino-4-(methylsulfanyl)butanoic acid
Traditional IUPAC NameL-methionine
Chemical FormulaC5H11NO2S
SMILES[H]OC(=O)[C@@]([H])(N([H])[H])C([H])([H])C([H])([H])SC([H])([H])[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as methionine and derivatives. Methionine and derivatives are compounds containing methionine or a derivative thereof resulting from reaction of methionine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentMethionine and derivatives
Alternative Parents
Substituents
  • Methionine or derivatives
  • Alpha-amino acid
  • L-alpha-amino acid
  • Thia fatty acid
  • Fatty acid
  • Fatty acyl
  • Amino acid
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Thioether
  • Sulfenyl compound
  • Dialkylthioether
  • Amine
  • Organic oxygen compound
  • Primary amine
  • Organosulfur compound
  • Organooxygen compound
  • Organonitrogen compound
  • Organic nitrogen compound
  • Primary aliphatic amine
  • Carbonyl group
  • Organopnictogen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point284 °C
Experimental Properties
PropertyValueReference
Water Solubility56.6 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)]PhysProp
LogP-1.87 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility23.9 g/LALOGPS
logP-1.9ALOGPS
logP-2.2ChemAxon
logS-0.8ALOGPS
pKa (Strongest Acidic)2.53ChemAxon
pKa (Strongest Basic)9.5ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area63.32 ŲChemAxon
Rotatable Bond Count4ChemAxon
Refractivity37.59 m³·mol⁻¹ChemAxon
Polarizability15.5 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Biotin BiosynthesisPW002380 ThumbThumb?image type=greyscaleThumb?image type=simple
Lipoic acid metabolismPW002499 ThumbThumb?image type=greyscaleThumb?image type=simple
Methionine metabolism and salvagePW002384 ThumbThumb?image type=greyscaleThumb?image type=simple
One Carbon Pool by Folate IPW002468 ThumbThumb?image type=greyscaleThumb?image type=simple
beta-Alanine metabolismPW002381 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Cysteine and methionine metabolismec00270 Map00270
Lipoic acid metabolismec00785 Map00785
beta-Alanine metabolismec00410 Map00410
SMPDB Reactions
Dethiobiotin + S-Adenosyl-L-methionine + Reduced ferredoxin + a sulfurated [sulfur carrier]  → Biotin + L-Methionine + 5'-Deoxyadenosine + an unsulfurated [sulfur carrier] + Oxidized ferredoxin
L-Methionine + Adenosine triphosphate + waterphosphate + Pyrophosphate + S-Adenosyl-L-methionine
Homocysteine + 5-Methyltetrahydropteroyltri-L-glutamateL-Methionine + Tetrahydropteroyltri-L-glutamate
4-Methylthio-2-oxobutanoate + L-PhenylalanineL-Methionine + 2-Ketobutyric acid
5-Methyltetrahydrofolic acid + HomocysteineTetrahydrofolic acid + L-Methionine
KEGG Reactions
4-Methylthio-2-oxobutanoate + L-Glutamic acidL-Methionine + Oxoglutaric acid
L-Homocysteine + 5-Methyltetrahydropteroyltri-L-glutamic acidL-Methionine + Tetrahydropteroyltri-L-glutamate
L-Homocysteine + S-AdenosylmethionineL-Methionine + S-Adenosylhomocysteine + hydron
L-Methionine + Adenosine triphosphate + waterPyrophosphate + phosphate + S-Adenosylmethionine
L-Homocysteine + 5-Methyltetrahydrofolic acidL-Methionine + 5,6,7,8-Tetrahydrofolic acid + hydron
Concentrations
Intracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
344 ± 7 µM YPD mediaaerobicBaker's yeastPMID: 7654310
344 ± 7 µM YPG mediaaerobicBaker's yeastPMID: 7654310
69 ± 1 µM SD mediaaerobicBaker's yeastPMID: 7654310
69 ± 1 µM SG mediaaerobicBaker's yeastPMID: 7654310
275 ± 5 µM M (molasses)aerobicBaker's yeastPMID: 7654310
137 ± 3 µM MA (molasses)aerobicBaker's yeastPMID: 7654310
69 ± 1 µM MB (molasses)aerobicBaker's yeastPMID: 7654310
137 ± 3 µM MAB (molasses)aerobicBaker's yeastPMID: 7654310
592 ± 30 µM YEB media with 0.5 mM glucoseaerobicBaker's yeastExperimentally Determined
Not Available
160 ± 34 µM Synthetic medium with 20 g/L glucoseaerobicBaker's yeastPMID: 12584756
Conversion Details Here
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • Martinez-Force, E., Benitez, T. (1995). "Effects of varying media, temperature, and growth rates on the intracellular concentrations of yeast amino acids." Biotechnol Prog 11:386-392.7654310
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • White, W. H., Gunyuzlu, P. L., Toyn, J. H. (2001). "Saccharomyces cerevisiae is capable of de Novo pantothenic acid biosynthesis involving a novel pathway of beta-alanine production from spermine." J Biol Chem 276:10794-10800.11154694
  • Cherest, H., Eichler, F., Robichon-Szulmajster, H. (1969). "Genetic and regulatory aspects of methionine biosynthesis in Saccharomyces cerevisiae." J Bacteriol 97:328-336.5764336
  • Pirkov, I., Norbeck, J., Gustafsson, L., Albers, E. (2008). "A complete inventory of all enzymes in the eukaryotic methionine salvage pathway." FEBS J 275:4111-4120.18625006
  • Hans, M. A., Heinzle, E., Wittmann, C. (2003). "Free intracellular amino acid pools during autonomous oscillations in Saccharomyces cerevisiae." Biotechnol Bioeng 82:143-151.12584756
  • Mulet, J. M., Alemany, B., Ros, R., Calvete, J. J., Serrano, R. (2004). "Expression of a plant serine O-acetyltransferase in Saccharomyces cerevisiae confers osmotic tolerance and creates an alternative pathway for cysteine biosynthesis." Yeast 21:303-312.15042590
  • Chiang, P. K., Cantoni, G. L. (1977). "Activation of methionine for transmethylation. Purification of the S-adenosylmethionine synthetase of bakers' yeast and its separation into two forms." J Biol Chem 252:4506-4513.194884
  • Nookaew, I., Jewett, M. C., Meechai, A., Thammarongtham, C., Laoteng, K., Cheevadhanarak, S., Nielsen, J., Bhumiratana, S. (2008). "The genome-scale metabolic model iIN800 of Saccharomyces cerevisiae and its validation: a scaffold to query lipid metabolism." BMC Syst Biol 2:71.18687109
  • Suliman, H. S., Sawyer, G. M., Appling, D. R., Robertus, J. D. (2005). "Purification and properties of cobalamin-independent methionine synthase from Candida albicans and Saccharomyces cerevisiae." Arch Biochem Biophys 441:56-63.16083849
  • Thomas, D., Becker, A., Surdin-Kerjan, Y. (2000). "Reverse methionine biosynthesis from S-adenosylmethionine in eukaryotic cells." J Biol Chem 275:40718-40724.11013242
  • Csaikl, U., Csaikl, F. (1986). "Molecular cloning and characterization of the MET6 gene of Saccharomyces cerevisiae." Gene 46:207-214.3542720
Synthesis Reference:Boy, Matthias; Klein, Daniela; Schroeder, Hartwig. Method for the production and recovery of methionine. PCT Int. Appl. (2005), 34 pp.
External Links:
ResourceLink
CHEBI ID16643
HMDB IDHMDB00696
Pubchem Compound ID6137
Kegg IDC00073
ChemSpider ID5907
FOODB IDFDB012683
WikipediaMethionine
BioCyc IDMET

Enzymes

General function:
Involved in protein binding
Specific function:
Catalyzes the reversible oxidation-reduction of the R- enantiomer of free methionine sulfoxide to methionine. Does not act on S-enantiomer of free methionine sulfoxide or R-enantiomer of dabsylated methionine sulfoxide. Involved in protection against oxidative stress
Gene Name:
Not Available
Uniprot ID:
P36088
Molecular weight:
19734.19922
Reactions
L-methionine + thioredoxin disulfide + H(2)O → L-methionine (R)-S-oxide + thioredoxin.
General function:
Involved in pyridoxal phosphate binding
Specific function:
Transforms O-acetylhomoserine into homocysteine and O- acetylserine into cysteine
Gene Name:
MET17
Uniprot ID:
P06106
Molecular weight:
48671.39844
Reactions
O-acetyl-L-homoserine + methanethiol → L-methionine + acetate.
O(3)-acetyl-L-serine + H(2)S → L-cysteine + acetate.
General function:
Involved in catalytic activity
Specific function:
Dethiobiotin + sulfur + 2 S-adenosyl-L- methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine
Gene Name:
BIO2
Uniprot ID:
P32451
Molecular weight:
41883.80078
Reactions
Dethiobiotin + sulfur + 2 S-adenosyl-L-methionine → biotin + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
Specific function:
Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation
Gene Name:
MET6
Uniprot ID:
P05694
Molecular weight:
85859.20313
Reactions
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine → tetrahydropteroyltri-L-glutamate + L-methionine.
General function:
Involved in nucleotide binding
Specific function:
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Gene Name:
MSM1
Uniprot ID:
P22438
Molecular weight:
66733.89844
Reactions
ATP + L-methionine + tRNA(Met) → AMP + diphosphate + L-methionyl-tRNA(Met).
General function:
Involved in nucleotide binding
Specific function:
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Gene Name:
MES1
Uniprot ID:
P00958
Molecular weight:
85677.39844
Reactions
ATP + L-methionine + tRNA(Met) → AMP + diphosphate + L-methionyl-tRNA(Met).
General function:
Involved in methionine adenosyltransferase activity
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP
Gene Name:
SAM1
Uniprot ID:
P10659
Molecular weight:
41818.0
Reactions
ATP + L-methionine + H(2)O → phosphate + diphosphate + S-adenosyl-L-methionine.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (Probable)
Gene Name:
LIP5
Uniprot ID:
P32875
Molecular weight:
46246.80078
Reactions
Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine → protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine.
General function:
Involved in transferase activity, transferring nitrogenous groups
Specific function:
Has aromatic amino acid transaminase activity and kynurenine aminotransferase activity
Gene Name:
ARO9
Uniprot ID:
P38840
Molecular weight:
58527.0
Reactions
An aromatic amino acid + 2-oxoglutarate → an aromatic oxo acid + L-glutamate.
General function:
Involved in homocysteine S-methyltransferase activity
Specific function:
Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S- methylmethionine (SMM) to methionine
Gene Name:
MHT1
Uniprot ID:
Q12525
Molecular weight:
36714.5
Reactions
S-methyl-L-methionine + L-homocysteine → 2 L-methionine.
General function:
Involved in homocysteine S-methyltransferase activity
Specific function:
Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S- methylmethionine (SMM) to methionine
Gene Name:
SAM4
Uniprot ID:
Q08985
Molecular weight:
36668.19922
Reactions
S-methyl-L-methionine + L-homocysteine → 2 L-methionine.
General function:
Involved in oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Specific function:
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Also able to reduce dimethyl sulfoxide (DMSO) as well, with DMS as the product
Gene Name:
MXR1
Uniprot ID:
P40029
Molecular weight:
21140.69922
Reactions
Peptide-L-methionine + thioredoxin disulfide + H(2)O → peptide-L-methionine (S)-S-oxide + thioredoxin.
L-methionine + thioredoxin disulfide + H(2)O → L-methionine (S)-S-oxide + thioredoxin.
General function:
Involved in aminopeptidase activity
Specific function:
Removes the amino-terminal methionine from nascent proteins
Gene Name:
MAP1
Uniprot ID:
Q01662
Molecular weight:
43373.0
General function:
Involved in aminopeptidase activity
Specific function:
Removes the amino-terminal methionine from nascent proteins
Gene Name:
MAP2
Uniprot ID:
P38174
Molecular weight:
47502.19922
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP
Gene Name:
SAM2
Uniprot ID:
P19358
Molecular weight:
42255.5
Reactions
ATP + L-methionine + H(2)O → phosphate + diphosphate + S-adenosyl-L-methionine.
General function:
Involved in peptide-methionine-(S)-S-oxide reductase activity
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
P25566
Molecular weight:
19278.80078
Reactions
Peptide-L-methionine + thioredoxin disulfide + H(2)O → peptide-L-methionine (R)-S-oxide + thioredoxin.

Transporters

General function:
Involved in transport
Specific function:
Permease for various amino acids as well as for GABA. Can also transport L-cysteine and beta-alanine
Gene Name:
GAP1
Uniprot ID:
P19145
Molecular weight:
65654.89844
General function:
Involved in transport
Specific function:
High affinity transport of glutamine. Also transport Leu, Ser, Thr, Cys, Met and Asn
Gene Name:
GNP1
Uniprot ID:
P48813
Molecular weight:
73597.39844
General function:
Involved in transport
Specific function:
Permease for leucine, valine and isoleucine. Also transports cysteine, methionine, phenyalanine, tyrosine and tryptophan
Gene Name:
BAP2
Uniprot ID:
P38084
Molecular weight:
67669.60156
General function:
Involved in transport
Specific function:
Involved in transport of isoleucine, leucine, valine, cysteine, methionine, phenylalanine, tyrosine and tryptophan
Gene Name:
BAP3
Uniprot ID:
P41815
Molecular weight:
67364.39844
General function:
Involved in transport
Specific function:
Broad substrate range permease which transports asparagine and glutamine with intermediate specificity. Also transports Ala, Cys, Gly, Ile, Leu, Met, Phe, Ser, Thr, Tyr and Val. Important for the utilization of amino acids as a nitrogen source
Gene Name:
AGP1
Uniprot ID:
P25376
Molecular weight:
69670.70313
General function:
Involved in transport
Specific function:
Very low affinity permease for methionine
Gene Name:
MUP3
Uniprot ID:
P38734
Molecular weight:
60619.10156
General function:
Involved in transport
Specific function:
High affinity permease for methionine
Gene Name:
MUP1
Uniprot ID:
P50276
Molecular weight:
63220.80078