Record Information
Version2.0
Creation Date2012-05-31 13:54:59 -0600
Update Date2015-09-13 12:56:12 -0600
Secondary Accession Numbers
  • ECMDB02005
Identification
Name:Methionine sulfoxide
DescriptionMethionine sulfoxide is a member of the chemical class known as Alpha Amino Acids and Derivatives. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon).Methionine is an amino acid susceptible to being oxidized to methionine sulfoxide (MetSO). The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductase (MSR), an enzyme present in almost all organisms. (PMID 20969952) Oxidation of methionine to methionine sulfoxide is a major oxidative stress product that reaches levels as high as 60% in cataract while being essentially absent from clear lenses. Methionine oxidation results in loss of protein function that can be reversed through the action of methionine sulfoxide reductase A (MsrA), which is implicated in oxidative stress protection and is an essential regulator of longevity in species ranging from Escherichia coli to mice. (PMID 15199188) A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. (PMID 10964927)
Structure
Thumb
Synonyms:
  • 2-amino-4-(methylsulfinyl)-Butanoate
  • 2-amino-4-(methylsulfinyl)-Butanoic acid
  • 2-amino-4-(Methylsulphinyl)-butanoate
  • 2-amino-4-(Methylsulphinyl)-butanoic acid
  • a-amino-g-(Methylsulfinyl)-butyrate
  • a-amino-g-(Methylsulfinyl)-butyric acid
  • a-amino-g-(Methylsulphinyl)-butyrate
  • a-amino-g-(Methylsulphinyl)-butyric acid
  • alpha-amino-gamma-(Methylsulfinyl)-butyrate
  • Alpha-amino-gamma-(methylsulfinyl)-Butyric acid
  • alpha-amino-gamma-(Methylsulphinyl)-butyrate
  • alpha-amino-gamma-(Methylsulphinyl)-butyric acid
  • DL-Methionine sulfoxide
  • DL-Methionine sulphoxide
  • H-Met(O)-OH
  • L-methionine (S)-S-oxide
  • L-methionine R-oxide
  • L-Methionine sulfoxide
  • L-Methionine sulfoxide 99+
  • L-Methionine sulphoxide
  • L-Methionine sulphoxide 99+
  • L-METHIONINEsulfoxide
  • L-METHIONINESULPHOXIDE
  • Methionine S-oxide
  • Methionine sulfoxide
  • Methionine sulphoxide
  • Methionine, S-oxide
  • MetSFX
  • S-oxide-methionine
  • α-amino-γ-(Methylsulfinyl)-butyrate
  • α-amino-γ-(Methylsulfinyl)-butyric acid
  • α-amino-γ-(Methylsulphinyl)-butyrate
  • α-amino-γ-(Methylsulphinyl)-butyric acid
Chemical Formula:C5H11NO3S
Weight:Average: 165.211
Monoisotopic: 165.045963913
InChI Key:QEFRNWWLZKMPFJ-UHFFFAOYSA-N
InChI:InChI=1S/C5H11NO3S/c1-10(9)3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)
CAS number:62697-73-8
IUPAC Name:(2S)-2-amino-4-methanesulfinylbutanoic acid
Traditional IUPAC Name:L-methionine sulfoxide
SMILES:CS(=O)CCC(N)C(O)=O
Chemical Taxonomy
Description belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentL-alpha-amino acids
Alternative Parents
Substituents
  • L-alpha-amino acid
  • Thia fatty acid
  • Fatty acid
  • Fatty acyl
  • Sulfoxide
  • Amino acid
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Sulfinyl compound
  • Carbonyl group
  • Organic oxygen compound
  • Organic nitrogen compound
  • Primary amine
  • Organosulfur compound
  • Organooxygen compound
  • Organonitrogen compound
  • Amine
  • Primary aliphatic amine
  • Organopnictogen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
State:Solid
Charge:0
Melting point:232 - 234 °C
Experimental Properties:
PropertyValueSource
LogP:-4.375PhysProp
Predicted Properties
PropertyValueSource
Water Solubility54 g/LALOGPS
logP-2.4ALOGPS
logP-4.6ChemAxon
logS-0.49ALOGPS
pKa (Strongest Acidic)1.74ChemAxon
pKa (Strongest Basic)9.11ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area80.39 ŲChemAxon
Rotatable Bond Count4ChemAxon
Refractivity39.34 m³·mol⁻¹ChemAxon
Polarizability15.98 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
EcoCyc Pathways:Not Available
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
7± 1 uMBL21 DE3Luria-Bertani (LB) mediaStationary phase cultures (overnight culture)Shake flask37 oCExperimentally Determined
Download Details
Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (Non-derivatized)splash10-004i-0900000000-6639ef576db5a01f8ee5View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (Non-derivatized)splash10-004i-0910000000-4231d540eda02eebe871View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (Non-derivatized)splash10-004i-0900000000-f0849e8acf9a3e1e2763View in MoNA
GC-MSGC-MS Spectrum - GC-MS (3 TMS)splash10-004i-1910000000-b7a64800b9e577e219d4View in MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-004i-1910000000-b7a64800b9e577e219d4View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-004i-0900000000-a5138c4f03667c81645cView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-004i-0910000000-b8f17a35f754f6a2adffView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-004i-0900000000-40d23196cb4ee1cad23fView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-00di-9400000000-cac8577601b69f1b723aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-00di-9000000000-43361da834d0b07907fdView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-00di-9000000000-6090b56aa5a22d72fb4fView in MoNA
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableView in JSpectraViewer
References
References:
  • Arias, D. G., Cabeza, M. S., Erben, E. D., Carranza, P. G., Lujan, H. D., Tellez Inon, M. T., Iglesias, A. A., Guerrero, S. A. (2011). "Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp." Free Radic Biol Med 50:37-46. Pubmed: 20969952
  • Boudier C, Cadene M, Bieth JG: Inhibition of neutrophil cathepsin G by oxidized mucus proteinase inhibitor. Effect of heparin. Biochemistry. 1999 Jun 29;38(26):8451-7. Pubmed: 10387091
  • Kantorow, M., Hawse, J. R., Cowell, T. L., Benhamed, S., Pizarro, G. O., Reddy, V. N., Hejtmancik, J. F. (2004). "Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress." Proc Natl Acad Sci U S A 101:9654-9659. Pubmed: 15199188
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Mashima R, Nakanishi-Ueda T, Yamamoto Y: Simultaneous determination of methionine sulfoxide and methionine in blood plasma using gas chromatography-mass spectrometry. Anal Biochem. 2003 Feb 1;313(1):28-33. Pubmed: 12576054
  • O'Donohue TL, Charlton CG, Thoa NB, Helke CJ, Moody TW, Pert A, Williams A, Miller RL, Jacobowitz DM: Release of alpha-melanocyte stimulating hormone into rat and human cerebrospinal fluid in vivo and from rat hypothalamus slices in vitro. Peptides. 1981 Spring;2(1):93-100. Pubmed: 7243627
  • Schallreuter KU: Functioning methionine-S-sulfoxide reductases A and B are present in human skin. J Invest Dermatol. 2006 May;126(5):947-9. Pubmed: 16619011
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference:Not Available
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID17016
HMDB IDHMDB02005
Pubchem Compound ID158980
Kegg IDC02989
ChemSpider ID824
Wikipedia IDMethionine sulfoxide
BioCyc IDCPD0-1959
EcoCyc IDCPD0-1959

Enzymes

General function:
Involved in oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Specific function:
Could have 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
Gene Name:
msrA
Uniprot ID:
P0A744
Molecular weight:
23315
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 peptide-methionine-(S)-S-oxide reductase activity
Specific function:
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin
Gene Name:
msrB
Uniprot ID:
P0A746
Molecular weight:
15451
Reactions
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
General function:
Involved in electron carrier activity
Specific function:
Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin
Gene Name:
trxC
Uniprot ID:
P0AGG4
Molecular weight:
15555
Reactions
Protein dithiol + NAD(P)(+) = protein disulfide + NAD(P)H.
General function:
Involved in oxidoreductase activity
Specific function:
This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin
Gene Name:
bisC
Uniprot ID:
P20099
Molecular weight:
85850
General function:
Involved in electron carrier activity
Specific function:
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions
Gene Name:
trxA
Uniprot ID:
P0AA25
Molecular weight:
11807

Transporters

General function:
Involved in transporter activity
Specific function:
Non-specific porin
Gene Name:
ompN
Uniprot ID:
P77747
Molecular weight:
41220
General function:
Involved in transporter activity
Specific function:
Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes
Gene Name:
phoE
Uniprot ID:
P02932
Molecular weight:
38922
General function:
Involved in transporter activity
Specific function:
OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2
Gene Name:
ompF
Uniprot ID:
P02931
Molecular weight:
39333
General function:
Involved in transporter activity
Specific function:
Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane
Gene Name:
ompC
Uniprot ID:
P06996
Molecular weight:
40368