Methionine sulfoxide (PAMDB000428)

IdentificationTaxonomyPhysical PropertiesBiological PropertiesSpectraConcentrationsLinksReferencesEnzymes Transporters
Proteins (3280)
Record Information
Version 1.0
Update Date 1/22/2018 12:54:54 PM
Metabolite IDPAMDB000428
Identification
Name: Methionine sulfoxide
Description:Methionine 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 Pseudomonas aeruginosa to mice. (PMID 15199188) A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Pseudomonas aeruginosa. (PMID 10964927)
Structure
Thumb
🔍MOLSDFPDBSMILESInChIView Structure
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
Average Molecular Weight: 165.211
Monoisotopic Molecular Weight: 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:2-amino-4-methanesulfinylbutanoic acid
Traditional IUPAC Name: DL-methionine sulfoxide
SMILES:CS(=O)CCC(N)C(O)=O
Chemical Taxonomy
Taxonomy DescriptionThis compound belongs to the class of organic compounds known as alpha amino acids. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon).
Kingdom Organic compounds
Super ClassOrganic acids and derivatives
Class Carboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct Parent Alpha amino acids
Alternative Parents
Substituents
  • Alpha-amino acid
  • Thia fatty acid
  • Amino fatty acid
  • Fatty acyl
  • Fatty acid
  • Sulfoxide
  • Sulfinyl compound
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Hydrocarbon derivative
  • Primary amine
  • Organosulfur compound
  • Organooxygen compound
  • Organonitrogen compound
  • Primary aliphatic amine
  • Carbonyl group
  • Amine
  • Aliphatic acyclic compound
Molecular Framework Aliphatic 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 Solubility54.0 mg/mLALOGPS
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 Å2ChemAxon
Rotatable Bond Count4ChemAxon
Refractivity39.34 m3·mol-1ChemAxon
Polarizability16.04 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations: Cytoplasm
Reactions:
Methionine sulfoxide + Reduced Thioredoxin > Water + L-Methionine + Oxidized Thioredoxin
Hydrogen peroxide + L-Methionine > Water + Methionine sulfoxide
Pathways: Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)splash10-004i-0900000000-6639ef576db5a01f8ee5View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)splash10-004i-0910000000-4231d540eda02eebe871View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)splash10-004i-0900000000-f0849e8acf9a3e1e2763View in MoNA
GC-MSGC-MS Spectrum - GC-MS (3 TMS)splash10-004i-1910000000-b7a64800b9e577e219d4View 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
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, NegativeNot Available
1D NMR1H NMR SpectrumNot Available
1D NMR1H NMR SpectrumNot Available
1D NMR13C NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
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 ID49033
HMDB IDHMDB02005
Pubchem Compound ID847
Kegg IDC02989
ChemSpider ID824
Wikipedia IDNot Available
BioCyc IDCPD0-1959
EcoCyc IDCPD0-1959

Enzymes

Protein Details
• Peptide methionine sulfoxide reductase msrA
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
Locus Tag:
PA5018
Molecular weight:
23.5 kDa
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.
Protein Details
• Peptide methionine sulfoxide reductase msrB
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
Locus Tag:
PA2827
Molecular weight:
14.8 kDa
Reactions
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
Protein Details
• Thioredoxin-1
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
Locus Tag:
PA5240
Molecular weight:
11.9 kDa

Transporters