Record Information
Version2.0
Creation Date2012-05-31 09:56:47 -0600
Update Date2015-09-13 12:56:06 -0600
Secondary Accession Numbers
  • ECMDB00078
Identification
Name:Cysteinylglycine
Description:Cysteinylglycine is a naturally occurring dipeptide. It is derived from the breakdown of glutathione (a tripeptide).
Structure
Thumb
Synonyms:
  • Cys-Gly
  • L-Cysteinyl-glycine
  • L-Cysteinylglycine
  • N-Cysteinyl Glycine
  • N-Cysteinyl-Glycine
  • N-L-Cysteinyl-Glycine
  • N-L-Cysteinylglycine
Chemical Formula:C5H10N2O3S
Weight:Average: 178.21
Monoisotopic: 178.041212886
InChI Key:ZUKPVRWZDMRIEO-VKHMYHEASA-N
InChI:InChI=1S/C5H10N2O3S/c6-3(2-11)5(10)7-1-4(8)9/h3,11H,1-2,6H2,(H,7,10)(H,8,9)/t3-/m0/s1
CAS number:19246-18-5
IUPAC Name:2-[(2R)-2-amino-3-sulfanylpropanamido]acetic acid
Traditional IUPAC Name:cysteinylglycine
SMILES:N[C@@H](CS)C(=O)NCC(O)=O
Chemical Taxonomy
DescriptionThis compound belongs to the class of chemical entities known as dipeptides. These are organic compounds containing a sequence of exactly two alpha-amino acids joined by a peptide bond.
KingdomChemical entities
Super ClassOrganic compounds
ClassOrganic acids and derivatives
Sub ClassCarboxylic acids and derivatives
Direct ParentDipeptides
Alternative Parents
Substituents
  • Alpha-dipeptide
  • N-acyl-alpha-amino acid
  • N-acyl-alpha amino acid or derivatives
  • Alpha-amino acid amide
  • Cysteine or derivatives
  • Alpha-amino acid or derivatives
  • Amino acid or derivatives
  • Amino acid
  • Carboxamide group
  • Secondary carboxylic acid amide
  • Alkylthiol
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Organic nitrogen compound
  • Organonitrogen compound
  • Organooxygen compound
  • Organosulfur compound
  • Primary aliphatic amine
  • Primary amine
  • Hydrocarbon derivative
  • Carbonyl group
  • Organic oxide
  • Amine
  • Organopnictogen compound
  • Organic oxygen compound
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
State:Solid
Charge:0
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility6.25 mg/mLALOGPS
logP-2.6ALOGPS
logP-3.9ChemAxon
logS-1.5ALOGPS
pKa (Strongest Acidic)3.6ChemAxon
pKa (Strongest Basic)8.08ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count4ChemAxon
Polar Surface Area92.42 Å2ChemAxon
Rotatable Bond Count4ChemAxon
Refractivity41.03 m3·mol-1ChemAxon
Polarizability16.98 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
SMPDB Pathways:
Glutathione metabolismPW000833 Pw000833Pw000833 greyscalePw000833 simple
KEGG Pathways:
EcoCyc Pathways:Not Available
Concentrations
Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-MS (3 TMS)splash10-00di-2980000000-043097e8f1f3f47ff51fView in MoNA
GC-MSGC-MS Spectrum - GC-MSNot Available
GC-MSGC-MS Spectrum - GC-EI-TOFsplash10-00di-9440000000-ff8b27f3afc92193d83aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - ESI-ITFT , positivesplash10-004i-9700000000-6fba6043a24b724b037eView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-004i-5900000000-b9a1082799c427caf10bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-004i-9200000000-2b99992e97c6ecb4567bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a6u-9000000000-a8b591f7522fe16637fbView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-004i-2900000000-0173b5cf52bb61095c3aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00gl-7900000000-f8dc26c3e8b8ec327fc4View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0kh9-9100000000-410b0cc1b5e3f850b505View in MoNA
References
References:
  • Andersson A, Isaksson A, Brattstrom L, Hultberg B: Homocysteine and other thiols determined in plasma by HPLC and thiol-specific postcolumn derivatization. Clin Chem. 1993 Aug;39(8):1590-7. Pubmed: 8353942
  • Badiou S, Bellet H, Lehmann S, Cristol JP, Jaber S: Elevated plasma cysteinylglycine levels caused by cilastatin-associated antibiotic treatment. Clin Chem Lab Med. 2005;43(3):332-4. Pubmed: 15843241
  • Bald E, Glowacki R: Analysis of saliva for glutathione and metabolically related thiols by liquid chromatography with ultraviolet detection. Amino Acids. 2005 Jun;28(4):431-3. Epub 2005 May 20. Pubmed: 15900404
  • Duman BS, Ozturk M, Yilmazeri S, Hatemi H: Thiols, malonaldehyde and total antioxidant status in the Turkish patients with type 2 diabetes mellitus. Tohoku J Exp Med. 2003 Nov;201(3):147-55. Pubmed: 14649736
  • Ebisch IM, Peters WH, Thomas CM, Wetzels AM, Peer PG, Steegers-Theunissen RP: Homocysteine, glutathione and related thiols affect fertility parameters in the (sub)fertile couple. Hum Reprod. 2006 Jul;21(7):1725-33. Epub 2006 Mar 23. Pubmed: 16556671
  • Fiskerstrand T, Refsum H, Kvalheim G, Ueland PM: Homocysteine and other thiols in plasma and urine: automated determination and sample stability. Clin Chem. 1993 Feb;39(2):263-71. Pubmed: 8432015
  • Giustarini D, Lorenzini S, Rossi R, Chindamo D, Di Simplicio P, Marcolongo R: Altered thiol pattern in plasma of subjects affected by rheumatoid arthritis. Clin Exp Rheumatol. 2005 Mar-Apr;23(2):205-12. Pubmed: 15895891
  • Jacobsen DW, Gatautis VJ, Green R, Robinson K, Savon SR, Secic M, Ji J, Otto JM, Taylor LM Jr: Rapid HPLC determination of total homocysteine and other thiols in serum and plasma: sex differences and correlation with cobalamin and folate concentrations in healthy subjects. Clin Chem. 1994 Jun;40(6):873-81. Pubmed: 8087981
  • Josch C, Sies H, Akerboom TP: Hepatic mercapturic acid formation: involvement of cytosolic cysteinylglycine S-conjugate dipeptidase activity. Biochem Pharmacol. 1998 Sep 15;56(6):763-71. Pubmed: 9751082
  • Kagedal B, Kallberg M: Cysteinylglycine in urine determined by high-performance liquid chromatography. J Chromatogr. 1984 Jun 8;308:75-82. Pubmed: 6746837
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • 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
  • Mansoor MA, Svardal AM, Ueland PM: Determination of the in vivo redox status of cysteine, cysteinylglycine, homocysteine, and glutathione in human plasma. Anal Biochem. 1992 Feb 1;200(2):218-29. Pubmed: 1632485
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. Pubmed: 9554495
  • Perry TL, Hansen S: Cystinylglycine in plasma: diagnostic relevance for pyroglutamic acidemia, homocystinuria, and phenylketonuria. Clin Chim Acta. 1981 Nov 25;117(1):7-12. Pubmed: 7333014
  • Raijmakers MT, Roes EM, Zusterzeel PL, Steegers EA, Peters WH: Thiol status and antioxidant capacity in women with a history of severe pre-eclampsia. BJOG. 2004 Mar;111(3):207-12. Pubmed: 14961880
  • Reddy VB, Doss GA, Creighton M, Kochansky CJ, Vincent SH, Franklin RB, Karanam BV: Identification and metabolism of a novel dihydrohydroxy-S-glutathionyl conjugate of a peroxisome proliferator-activated receptor agonist, MK-0767 [(+/-)-5-[(2,4-dioxothiazolidin-5-yl)methyl]-2-methoxy-N-[[(4-trifluoromet hyl) phenyl]methyl]benzamide], in rats. Drug Metab Dispos. 2004 Oct;32(10):1154-61. Epub 2004 Jun 30. Pubmed: 15229171
  • Ueland PM, Mansoor MA, Guttormsen AB, Muller F, Aukrust P, Refsum H, Svardal AM: Reduced, oxidized and protein-bound forms of homocysteine and other aminothiols in plasma comprise the redox thiol status--a possible element of the extracellular antioxidant defense system. J Nutr. 1996 Apr;126(4 Suppl):1281S-4S. Pubmed: 8642471
  • Van Hove JL, Lazeyras F, Zeisel SH, Bottiglieri T, Hyland K, Charles HC, Gray L, Jaeken J, Kahler SG: One-methyl group metabolism in non-ketotic hyperglycinaemia: mildly elevated cerebrospinal fluid homocysteine levels. J Inherit Metab Dis. 1998 Dec;21(8):799-811. Pubmed: 9870205
  • Zappacosta B, Manni A, Persichilli S, Scribano D, Minucci A, Lazzaro D, De Sole P, Giardina B: HPLC analysis of some sulphur compounds in saliva: comparison between healthy subjects and periodontopathic patients. Clin Chim Acta. 2003 Dec;338(1-2):57-60. Pubmed: 14637266
  • Zinellu A, Carru C, Galistu F, Usai MF, Pes GM, Baggio G, Federici G, Deiana L: N-methyl-D-glucamine improves the laser-induced fluorescence capillary electrophoresis performance in the total plasma thiols measurement. Electrophoresis. 2003 Aug;24(16):2796-804. Pubmed: 12929176
Synthesis Reference:Holleman, James W. Synthesis of glutathione and cysteinylglycine by soluble enzymes of rat liver. Compt. rend. (1954), 238 1360-1.
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID4047
HMDB IDHMDB00078
Pubchem Compound ID439498
Kegg IDC01419
ChemSpider ID388596
Wikipedia IDNot Available
BioCyc IDCYS-GLY
EcoCyc IDCYS-GLY

Enzymes

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 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 gamma-glutamyltransferase activity
Specific function:
(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid
Gene Name:
ggt
Uniprot ID:
P18956
Molecular weight:
61768
Reactions
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.
Glutathione + H(2)O = L-cysteinylglycine + L-glutamate.
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 transporter activity
Specific function:
Part of the binding-protein-dependent transport system for dipeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
dppB
Uniprot ID:
P0AEF8
Molecular weight:
37497
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for dipeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
dppC
Uniprot ID:
P0AEG1
Molecular weight:
32308
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
oppB
Uniprot ID:
P0AFH2
Molecular weight:
33443
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
oppC
Uniprot ID:
P0AFH6
Molecular weight:
33022
General function:
Involved in nucleotide binding
Specific function:
Part of the binding-protein-dependent transport system for dipeptides. Probably responsible for energy coupling to the transport system
Gene Name:
dppD
Uniprot ID:
P0AAG0
Molecular weight:
35844
General function:
Involved in nucleotide binding
Specific function:
Part of the binding-protein-dependent transport system for dipeptides. Probably responsible for energy coupling to the transport system
Gene Name:
dppF
Uniprot ID:
P37313
Molecular weight:
37560
General function:
Involved in transporter activity
Specific function:
Dipeptide-binding protein of a transport system that can be subject to osmotic shock. DppA is also required for peptide chemotaxis
Gene Name:
dppA
Uniprot ID:
P23847
Molecular weight:
60293

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 transporter activity
Specific function:
Part of the binding-protein-dependent transport system for dipeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
dppB
Uniprot ID:
P0AEF8
Molecular weight:
37497
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for dipeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
dppC
Uniprot ID:
P0AEG1
Molecular weight:
32308
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
oppB
Uniprot ID:
P0AFH2
Molecular weight:
33443
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
oppC
Uniprot ID:
P0AFH6
Molecular weight:
33022
General function:
Involved in transporter activity
Specific function:
Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides
Gene Name:
sapB
Uniprot ID:
P0AGH3
Molecular weight:
36038
General function:
Involved in transporter activity
Specific function:
Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides
Gene Name:
sapC
Uniprot ID:
P0AGH5
Molecular weight:
31548
General function:
Involved in peptide transporter activity
Specific function:
Proton-dependent permease that transports di- and tripeptides. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate
Gene Name:
dtpB
Uniprot ID:
P36837
Molecular weight:
53575
General function:
Involved in peptide transporter activity
Specific function:
Probable proton-dependent permease that transports di- and tripeptides. Shows significantly higher specificity towards dipeptides
Gene Name:
yjdL
Uniprot ID:
P39276
Molecular weight:
53054
General function:
Involved in peptide transporter activity
Specific function:
Probable proton-dependent permease that transports dipeptides
Gene Name:
dtpD
Uniprot ID:
P75742
Molecular weight:
54158
General function:
Involved in peptide transporter activity
Specific function:
Proton-dependent permease that transports di- and tripeptides as well as structurally related peptidomimetics such as aminocephalosporins into the cell. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate
Gene Name:
dtpA
Uniprot ID:
P77304
Molecular weight:
53991
General function:
Involved in nucleotide binding
Specific function:
Part of the binding-protein-dependent transport system for dipeptides. Probably responsible for energy coupling to the transport system
Gene Name:
dppD
Uniprot ID:
P0AAG0
Molecular weight:
35844
General function:
Involved in transporter activity
Specific function:
Non-specific porin
Gene Name:
ompN
Uniprot ID:
P77747
Molecular weight:
41220
General function:
Involved in nucleotide binding
Specific function:
Part of the binding-protein-dependent transport system for dipeptides. Probably responsible for energy coupling to the transport system
Gene Name:
dppF
Uniprot ID:
P37313
Molecular weight:
37560
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:
Dipeptide-binding protein of a transport system that can be subject to osmotic shock. DppA is also required for peptide chemotaxis
Gene Name:
dppA
Uniprot ID:
P23847
Molecular weight:
60293
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