Record Information
Version2.0
Creation Date2012-05-31 10:27:32 -0600
Update Date2015-09-13 12:56:08 -0600
Secondary Accession Numbers
  • ECMDB00574
Identification
Name:L-Cysteine
DescriptionCysteine is a naturally occurring, sulfur-containing amino acid that is found in most proteins, although only in small quantities. Cysteine is unique amongst the twenty natural amino acids as it contains a thiol group. Thiol groups can undergo oxidation/reduction (redox) reactions; when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond. This reaction is reversible: as reduction of this disulphide bond regenerates two cysteine molecules. The disulphide bonds of cystine are crucial to defining the structures of many proteins. Cysteine is often involved in electron-transfer reactions, and help the enzyme catalyze its reaction. Cysteine is also part of the antioxidant glutathione. Oxidation of cysteine can produce a disulfide bond with another thiol, or further oxidation can produce sulphfinic or sulfonic acids. The cysteine thiol group is also a nucleophile and can undergo addition and substitution reactions. Thiol groups become much more reactive when they are ionized, and cysteine residues in proteins have pKa values close to neutrality, so are often in their reactive thiolate form in the cell. The thiol group also has a high affinity for heavy metals and proteins containing cysteine will bind metals such as mercury, lead and cadmium tightly.Due to this ability to undergo redox reactions, cysteine has antioxidant properties. Cysteine is important in energy metabolism. (http://www.dcnutrition.com/AminoAcids/)
Structure
Thumb
Synonyms:
  • (+)-2-Amino-3-mercaptopropionate
  • (+)-2-Amino-3-mercaptopropionic acid
  • (2R)-2-amino-3-mercaptopropanoate
  • (2R)-2-amino-3-mercaptopropanoic acid
  • (2R)-2-amino-3-sulfanylpropanoate
  • (2R)-2-amino-3-sulfanylpropanoic acid
  • (2R)-2-amino-3-sulphanylpropanoate
  • (2R)-2-amino-3-sulphanylpropanoic acid
  • (R)-(+)-cysteine
  • (R)-2-amino-3-mercapto-Propanoate
  • (R)-2-amino-3-mercapto-Propanoic acid
  • (R)-2-Amino-3-mercaptopropanoate
  • (R)-2-Amino-3-mercaptopropanoic acid
  • (R)-cysteine
  • 2-Amino-3-mercaptopropanoate
  • 2-Amino-3-mercaptopropanoic acid
  • 2-Amino-3-mercaptopropionate
  • 2-Amino-3-mercaptopropionic acid
  • 3-Mercapto-L-Alanine
  • a-amino-b-Thiolpropionate
  • a-amino-b-Thiolpropionic acid
  • Acetylcysteine
  • Alpha-Amino-beta-thiolpropionate
  • Alpha-Amino-beta-thiolpropionic acid
  • B-Mercaptoalanine
  • Beta-Mercaptoalanine
  • C
  • Carbocysteine
  • Cisteina
  • Cisteinum
  • Cys
  • Cystein
  • Cysteine
  • Cysteinum
  • Free cysteine
  • Half-cystine
  • L Cysteine
  • L-(+)-Cysteine
  • L-2-Amino-3-mercaptopropanoate
  • L-2-Amino-3-mercaptopropanoic acid
  • L-2-Amino-3-mercaptopropionate
  • L-2-Amino-3-mercaptopropionic acid
  • L-Cystein
  • L-Cysteine
  • Polycysteine
  • Thioserine
  • α-amino-β-Thiolpropionate
  • α-amino-β-Thiolpropionic acid
  • β-Mercaptoalanine
Chemical Formula:C3H7NO2S
Weight:Average: 121.158
Monoisotopic: 121.019749163
InChI Key:XUJNEKJLAYXESH-REOHCLBHSA-N
InChI:InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
CAS number:52-90-4
IUPAC Name:(2R)-2-amino-3-sulfanylpropanoic acid
Traditional IUPAC Name:L-cysteine
SMILES:N[C@@H](CS)C(O)=O
Chemical Taxonomy
Description belongs to the class of organic compounds known as cysteine and derivatives. Cysteine and derivatives are compounds containing cysteine or a derivative thereof resulting from reaction of cysteine 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 ParentCysteine and derivatives
Alternative ParentsNot Available
SubstituentsNot Available
Molecular FrameworkAliphatic acyclic compounds
External DescriptorsNot Available
Physical Properties
State:Solid
Charge:0
Melting point:220 °C
Experimental Properties:
PropertyValueSource
Water Solubility:277 mg/mL at 25 oC [BEILSTEIN]; 277.0 mg/mL [BEILSTEIN]PhysProp
LogP:-2.49 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility23.1 g/LALOGPS
logP-2.6ALOGPS
logP-2.8ChemAxon
logS-0.72ALOGPS
pKa (Strongest Acidic)2.35ChemAxon
pKa (Strongest Basic)9.05ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area63.32 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity28.22 m³·mol⁻¹ChemAxon
Polarizability11.41 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
Cysteinylglycine + Water > L-Cysteine + Glycine
Adenosine triphosphate + L-Cysteine + Water > ADP + Hydrogen ion + Phosphate + L-Cysteine
Adenosine triphosphate + L-Cysteine + Water > ADP + Hydrogen ion + Phosphate + L-Cysteine
L-Cysteine + SufSE sulfur acceptor complex > L-Alanine + SufSE with bound sulfur
O-Acetylserine + Hydrogen sulfide <> Acetic acid + L-Cysteine + Hydrogen ion
L-Cysteine + Water > Hydrogen sulfide + Ammonium + Pyruvic acid
Adenosine triphosphate + L-Cysteine + tRNA(Cys) + tRNA(Cys) <> Adenosine monophosphate + L-Cysteinyl-tRNA(Cys) + Pyrophosphate + L-Cysteinyl-tRNA(Cys)
L-Cysteine + IscS sulfur acceptor protein > L-Alanine + IscS with bound sulfur
Adenosine triphosphate + L-Cysteine + L-Glutamate <> ADP + gamma-Glutamylcysteine + Hydrogen ion + Phosphate
D-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine > 4-Phosphopantothenoylcysteine + Cytidine monophosphate + Hydrogen ion + Pyrophosphate
L-Cysteine + O-Succinyl-L-homoserine <> L-Cystathionine + Hydrogen ion + Succinic acid
L-Cysteine + Water <> Hydrogen sulfide + Pyruvic acid + Ammonia
Adenosine triphosphate + L-Glutamate + L-Cysteine <> ADP + Phosphate + gamma-Glutamylcysteine
L-Cysteine + alpha-Ketoglutarate <> 3-Mercaptopyruvic acid + DL-Glutamic acid
O-Acetylserine + Hydrogen sulfide <> L-Cysteine + Acetic acid
Cysteinylglycine + Water <> L-Cysteine + Glycine
Cystathionine + Succinic acid <> O-Succinyl-L-homoserine + L-Cysteine
o-acetyl-l-homoserine + L-Cysteine <> L-Cystathionine + Acetic acid
O-Succinyl-L-homoserine + L-Cysteine <> L-Cystathionine + Succinic acid
Adenosine triphosphate + L-Cysteine + tRNA(Cys) <> Adenosine monophosphate + Pyrophosphate + L-Cysteinyl-tRNA(Cys)
Adenosine triphosphate + D-4'-Phosphopantothenate + L-Cysteine <> Adenosine monophosphate + Pyrophosphate + 4-Phosphopantothenoylcysteine
Cytidine triphosphate + D-4'-Phosphopantothenate + L-Cysteine <> Cytidine monophosphate + Pyrophosphate + 4-Phosphopantothenoylcysteine
O-Acetylserine + Thiosulfate + Thioredoxin + Hydrogen ion <> L-Cysteine + Sulfite + Thioredoxin disulfide + Acetic acid
[Enzyme]-cysteine + L-Cysteine <> [Enzyme]-S-sulfanylcysteine + L-Alanine
Oxoglutaric acid + L-Cysteine > L-Glutamate + 3-Mercaptopyruvic acid
L-Cysteine + L-Glutamate + Adenosine triphosphate > Hydrogen ion + gamma-Glutamylcysteine + Phosphate + ADP
L-Cysteine + Water > Pyruvic acid + Ammonia + Hydrogen sulfide + Hydrogen ion
L-Cysteine + O-Succinyl-L-homoserine > Hydrogen ion + Succinic acid + L-Cystathionine
L-Cysteine + a sulfur acceptor + Hydrogen ion L-Alanine + <i>S</i>-sulfanyl-[acceptor]
L-Cysteine + Adenosine triphosphate + Water > L-Cysteine + ADP + Phosphate + Hydrogen ion
L-Cysteine + Adenosine triphosphate + Water > L-Cysteine + ADP + Phosphate + Hydrogen ion
L-Cysteine + L-Cysteine-Desulfurases > L-Alanine + Persulfurated-L-cysteine-desulfurases
Cytidine triphosphate + (R)-4'-phosphopantothenate + L-Cysteine > Cytidine monophosphate + Pyrophosphate + 4-Phosphopantothenoylcysteine
O-Acetylserine + Hydrogen sulfide > L-Cysteine + Acetic acid
Adenosine triphosphate + L-Glutamate + L-Cysteine > ADP + Inorganic phosphate + gamma-Glutamylcysteine
L-Cysteine + acceptor > L-Alanine + S-sulfanyl-acceptor
O-Succinyl-L-homoserine + L-Cysteine > L-Cystathionine + Succinic acid
Adenosine triphosphate + L-Cysteine + tRNA(Cys) > Adenosine monophosphate + Pyrophosphate + L-cysteinyl-tRNA(Cys)
L-Cysteine + 'activated' tRNA > L-Serine + tRNA containing a thionucleotide
L-Cysteine + 'Activated' tRNA <> L-Serine + tRNA containing a thionucleotide
L-Cysteine + an [L-cysteine desulfurase] L-cysteine persulfide > an [L-cysteine desulfurase] L-cysteine persulfide + L-Alanine + L-Alanine
L-Cysteine + tRNA(Cys) + Adenosine triphosphate + Hydrogen ion > Pyrophosphate + Adenosine monophosphate + L-cysteinyl-tRNA(Cys)
O-Acetylserine > Hydrogen ion + Acetic acid + L-Cysteine
O-Acetylserine + Hydrogen sulfide > Hydrogen ion + Acetic acid + L-Cysteine
L-Cysteine > Hydrogen ion + Hydrogen sulfide + 2-Aminoacrylic acid
Cytidine triphosphate + D-4'-Phosphopantothenate + L-Cysteine + D-4'-Phosphopantothenate > Cytidine monophosphate + Pyrophosphate + 4-Phosphopantothenoylcysteine + Cytidine monophosphate
D-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine + D-4'-Phosphopantothenate > Cytidine monophosphate + Pyrophosphate + Hydrogen ion + 4-Phosphopantothenoylcysteine + Cytidine monophosphate
L-Glutamic acid + Adenosine triphosphate + L-Cysteine + L-Glutamate > Adenosine diphosphate + Phosphate + Hydrogen ion + gamma-Glutamylcysteine + ADP
L-Cysteine + Adenosine triphosphate + Water > ADP + Phosphate + Hydrogen ion
L-Cysteine > Hydrogen sulfide + Hydrogen ion + 2-aminoprop-2-enoate
O-Acetylserine + Hydrogen sulfide <> Acetic acid + L-Cysteine + Hydrogen ion
Adenosine triphosphate + L-Cysteine + tRNA(Cys) <> Adenosine monophosphate + L-Cysteinyl-tRNA(Cys) + Pyrophosphate
O-Acetylserine + Hydrogen sulfide <> L-Cysteine + Acetic acid
[Enzyme]-cysteine + L-Cysteine <> [Enzyme]-S-sulfanylcysteine + L-Alanine
Cysteinylglycine + Water > L-Cysteine + Glycine
Adenosine triphosphate + L-Cysteine + L-Glutamate <> ADP + gamma-Glutamylcysteine + Hydrogen ion + Phosphate
D-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine >4 4-Phosphopantothenoylcysteine + Cytidine monophosphate + Hydrogen ion + Pyrophosphate
[Enzyme]-cysteine + L-Cysteine <> [Enzyme]-S-sulfanylcysteine + L-Alanine
Adenosine triphosphate + L-Cysteine + L-Glutamate <> ADP + gamma-Glutamylcysteine + Hydrogen ion + Phosphate
D-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine >4 4-Phosphopantothenoylcysteine + Cytidine monophosphate + Hydrogen ion + Pyrophosphate
More...

SMPDB Pathways:
Glutathione metabolismPW000833 ThumbThumb?image type=greyscaleThumb?image type=simple
Hydrogen Sulfide Biosynthesis IPW002066 ThumbThumb?image type=greyscaleThumb?image type=simple
L-alanine metabolismPW000788 ThumbThumb?image type=greyscaleThumb?image type=simple
L-cysteine degradationPW002110 ThumbThumb?image type=greyscaleThumb?image type=simple
Pantothenate and CoA biosynthesisPW000828 ThumbThumb?image type=greyscaleThumb?image type=simple
Secondary Metabolites: cysteine biosynthesis from serinePW000977 ThumbThumb?image type=greyscaleThumb?image type=simple
Sulfur metabolismPW000922 ThumbThumb?image type=greyscaleThumb?image type=simple
cysteine biosynthesisPW000800 ThumbThumb?image type=greyscaleThumb?image type=simple
glutathione metabolism IIPW001927 ThumbThumb?image type=greyscaleThumb?image type=simple
glutathione metabolism IIIPW002018 ThumbThumb?image type=greyscaleThumb?image type=simple
methionine biosynthesisPW000814 ThumbThumb?image type=greyscaleThumb?image type=simple
sulfur metabolism (butanesulfonate)PW000923 ThumbThumb?image type=greyscaleThumb?image type=simple
sulfur metabolism (butanesulfonate/phenylacetaldehyde)PW001012 ThumbThumb?image type=greyscaleThumb?image type=simple
sulfur metabolism (ethanesulfonate)PW000925 ThumbThumb?image type=greyscaleThumb?image type=simple
sulfur metabolism (isethionate)PW000926 ThumbThumb?image type=greyscaleThumb?image type=simple
sulfur metabolism (methanesulfonate)PW000927 ThumbThumb?image type=greyscaleThumb?image type=simple
sulfur metabolism (propanesulfonate)PW000924 ThumbThumb?image type=greyscaleThumb?image type=simple
tRNA Charging 2PW000803 ThumbThumb?image type=greyscaleThumb?image type=simple
tRNA chargingPW000799 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
204± 45 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) (4 TMS)splash10-00kb-0950000000-df7e91c95b610ff21c79View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (4 TMS)splash10-00kb-0940000000-aefe34765fb447090a23View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (4 TMS)splash10-00kb-0970000000-10a155c40ea499023052View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (Non-derivatized)splash10-00kb-0940000000-037a3a34651c3154b3b3View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (4 TMS)splash10-00di-9850000000-118c43e33861a6baa8d2View in MoNA
GC-MSGC-MS Spectrum - EI-B (Non-derivatized)splash10-014j-0690100000-0aeb88fd507505e6b718View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00kb-0950000000-df7e91c95b610ff21c79View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00kb-0940000000-aefe34765fb447090a23View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00kb-0970000000-10a155c40ea499023052View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00kb-0940000000-037a3a34651c3154b3b3View in MoNA
GC-MSGC-MS Spectrum - GC-EI-QQ (Non-derivatized)splash10-0uk9-5619100000-8cb2558373966174ced3View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-00di-9850000000-118c43e33861a6baa8d2View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0gi0-0960000000-03b2097de6f9637d29cbView in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-004l-9100000000-4553906a941a5e87ec97View in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, Positivesplash10-004i-9200000000-cfaf705cd0452d428454View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-00b9-9600000000-374c5872d68662832769View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-0a4i-9000000000-ddbd3df6b8dbb280ffbaView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-0a4i-9000000000-320a2c77443b80ebf733View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0089-0900000000-9dcd3d757c5cd11eb18eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0udi-3900000000-212e081fe83ad70de0adView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-000i-9000000000-2eb01f41c225f614db24View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-001i-0900000000-a19834eb7cb9f211fdf2View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00di-0900000000-2458f2587761e779ed93View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0a4i-9000000000-77e590f0ed26f69b31c0View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0udi-3900000000-7b1857997392b006b95fView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0a4i-3900000000-bc268c27ed5706a4bbd2View in MoNA
LC-MS/MSLC-MS/MS Spectrum - CE-ESI-TOF (CE-system connected to 6210 Time-of-Flight MS, Agilent) , Positivesplash10-00di-0900000000-4573390bccc238e3c91bView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT , positivesplash10-0udi-3900000000-212e081fe83ad70de0adView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT , positivesplash10-0udi-3900000000-7b1857997392b006b95fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00b9-9600000000-4352a7b437c34c04d9f0View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-004i-9200000000-7b4cd034c717561c61ddView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-052f-9000000000-8f351cbca6ffed356a9bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00di-6900000000-51ba0df80cc33423420bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0079-9400000000-4aa2b707c391d5838d29View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-001i-9000000000-95c7672c7836c0fc51c9View in MoNA
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,1H] 2D NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableView in JSpectraViewer
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  • Santamaria I, Velasco G, Cazorla M, Fueyo A, Campo E, Lopez-Otin C: Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Res. 1998 Apr 15;58(8):1624-30. Pubmed: 9563472
  • Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
  • Taveau M, Bourg N, Sillon G, Roudaut C, Bartoli M, Richard I: Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components. Mol Cell Biol. 2003 Dec;23(24):9127-35. Pubmed: 14645524
  • 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
  • Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72. Pubmed: 18402659
  • 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
  • Yu FH, Westenbroek RE, Silos-Santiago I, McCormick KA, Lawson D, Ge P, Ferriera H, Lilly J, DiStefano PS, Catterall WA, Scheuer T, Curtis R: Sodium channel beta4, a new disulfide-linked auxiliary subunit with similarity to beta2. J Neurosci. 2003 Aug 20;23(20):7577-85. Pubmed: 12930796
  • Zhang JT, Li QX, Wang D, Zhu ZL, Yang YH, Cui DS, Wang MW, Sun XF: Up-regulation of PINCH in the stroma of oral squamous cell carcinoma predicts nodal metastasis. Oncol Rep. 2005 Dec;14(6):1519-22. Pubmed: 16273248
Synthesis Reference:Kumagai, Hidehiko; Tanaka, Hideyuki; Sejima, Shunsuke; Yamada, Hideaki. Elimination and replacement reactions of b-chloro-L-alanine by cysteine desulfhydrase from Aerobacter aerogenes. Agricultural and Biological Chemistry (1977), 41(10), 2071-5.
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID17561
HMDB IDHMDB00574
Pubchem Compound ID5862
Kegg IDC00097
ChemSpider ID5653
WikipediaL-Cysteine
BioCyc IDCYS
EcoCyc IDCYS
Ligand ExpoFCY

Enzymes

General function:
Involved in transferase activity
Specific function:
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Gene Name:
aspC
Uniprot ID:
P00509
Molecular weight:
43573
Reactions
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
General function:
Involved in pyridoxal phosphate binding
Specific function:
O(4)-succinyl-L-homoserine + L-cysteine = L- cystathionine + succinate
Gene Name:
metB
Uniprot ID:
P00935
Molecular weight:
41550
Reactions
O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate.
General function:
Involved in proteolysis
Specific function:
Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation
Gene Name:
pepN
Uniprot ID:
P04825
Molecular weight:
98918
Reactions
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
General function:
Involved in pyridoxal phosphate binding
Specific function:
L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate
Gene Name:
metC
Uniprot ID:
P06721
Molecular weight:
43212
Reactions
L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate.
General function:
Involved in metabolic process
Specific function:
Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for NAD, biotin and Fe-S cluster synthesis. Transfers sulfur on 'Cys-456' of thiI in a transpersulfidation reaction. Transfers sulfur on 'Cys-19' of tusA in a transpersulfidation reaction. Functions also as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate
Gene Name:
iscS
Uniprot ID:
P0A6B7
Molecular weight:
45089
Reactions
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
General function:
Involved in glutamate-cysteine ligase activity
Specific function:
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Gene Name:
gshA
Uniprot ID:
P0A6W9
Molecular weight:
58269
Reactions
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.
General function:
Involved in lyase activity
Specific function:
L-tryptophan + H(2)O = indole + pyruvate + NH(3)
Gene Name:
tnaA
Uniprot ID:
P0A853
Molecular weight:
52773
Reactions
L-tryptophan + H(2)O = indole + pyruvate + NH(3).
General function:
Involved in cysteine biosynthetic process from serine
Specific function:
O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate
Gene Name:
cysK
Uniprot ID:
P0ABK5
Molecular weight:
34489
Reactions
O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate.
3-chloro-L-alanine + thioglycolate = S-carboxymethyl-L-cysteine + chloride.
General function:
Involved in phosphopantothenate--cysteine ligase activity
Specific function:
Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine
Gene Name:
coaBC
Uniprot ID:
P0ABQ0
Molecular weight:
43438
Reactions
N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO(2).
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine.
General function:
Involved in hydrolase activity
Specific function:
Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids are hydrolyzed. Also shows cysteinylglycinase activity, which is sufficient for E.coli to utilize cysteinylglycine as a cysteine source
Gene Name:
pepD
Uniprot ID:
P15288
Molecular weight:
52915
Reactions
Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.
General function:
Involved in cysteine biosynthetic process from serine
Specific function:
Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product
Gene Name:
cysM
Uniprot ID:
P16703
Molecular weight:
32664
Reactions
O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate.
General function:
Involved in cysteine-tRNA ligase activity
Specific function:
ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Gene Name:
cysS
Uniprot ID:
P21888
Molecular weight:
52202
Reactions
ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).
General function:
Involved in transferase activity
Specific function:
Acts as a beta-cystathionase and as a repressor of the maltose regulon
Gene Name:
malY
Uniprot ID:
P23256
Molecular weight:
43641
Reactions
L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate.
General function:
Involved in aminopeptidase activity
Specific function:
Probably plays an important role in intracellular peptide degradation
Gene Name:
pepB
Uniprot ID:
P37095
Molecular weight:
46180
Reactions
Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln.
General function:
Involved in aminopeptidase activity
Specific function:
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place
Gene Name:
pepA
Uniprot ID:
P68767
Molecular weight:
54879
Reactions
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
General function:
Involved in metabolic process
Specific function:
Cysteine desulfurases mobilize the sulfur from L- cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo
Gene Name:
sufS
Uniprot ID:
P77444
Molecular weight:
44433
Reactions
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.
General function:
Involved in nucleotide binding
Specific function:
Somehow involved in the cytochrome D branch of aerobic respiration. Seems to be a component of a transport system
Gene Name:
cydC
Uniprot ID:
P23886
Molecular weight:
62920
General function:
Involved in nucleotide binding
Specific function:
Somehow involved in the cytochrome D branch of aerobic respiration. Seems to be a component of a transport system
Gene Name:
cydD
Uniprot ID:
P29018
Molecular weight:
65055
General function:
Involved in RNA binding
Specific function:
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by iscS
Gene Name:
thiI
Uniprot ID:
P77718
Molecular weight:
54973
Reactions
L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide.
[IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP.
General function:
Not Available
Specific function:
Participates in cysteine desulfuration mediated by sufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for sufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of sufS, an intermediate product of cysteine desulfuration process. Together with the sufBCD complex, it thereby enhances up to 50- fold, the cysteine desulfurase activity of sufS. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Does not affect the selenocysteine lyase activity of sufS
Gene Name:
sufE
Uniprot ID:
P76194
Molecular weight:
15800

Transporters

General function:
Involved in proteolysis
Specific function:
Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation
Gene Name:
pepN
Uniprot ID:
P04825
Molecular weight:
98918
Reactions
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
General function:
Involved in nucleotide binding
Specific function:
Probably part of a binding-protein-dependent transport system yecCS for an amino acid. Probably responsible for energy coupling to the transport system
Gene Name:
yecC
Uniprot ID:
P37774
Molecular weight:
27677
General function:
Involved in transporter activity
Specific function:
Probably part of the binding-protein-dependent transport system yecCS for an amino acid; probably responsible for the translocation of the substrate across the membrane
Gene Name:
yecS
Uniprot ID:
P0AFT2
Molecular weight:
24801
General function:
Involved in transporter activity
Specific function:
Non-specific porin
Gene Name:
ompN
Uniprot ID:
P77747
Molecular weight:
41220
General function:
Carbohydrate transport and metabolism
Specific function:
May be an export pump for cysteine and other metabolites of the cysteine pathway (such as N-acetyl-L-serine (NAS) and O- acetyl-L-serine (OAS)), and for other amino acids and their metabolites
Gene Name:
eamA
Uniprot ID:
P31125
Molecular weight:
32324
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
General function:
Signal transduction mechanisms
Specific function:
Exporter of O-acetylserine (OAS) and cysteine
Gene Name:
eamB
Uniprot ID:
P38101
Molecular weight:
21248
General function:
transporter activity
Specific function:
Part of a binding-protein-dependent transport system for cystine.
Gene Name:
fliY
Uniprot ID:
P0AEM9
Molecular weight:
29038