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Chemical Compound Review

Cys-Gly     2-[[(2S)-2-amino-3-sulfanyl...

Synonyms: CHEMBL371579, CHEBI:4047, AG-E-40614, HMDB00078, CTK0H6652, ...
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Disease relevance of C01419

  • In contrast, the E. coli enzyme was a nonselective enzyme that accommodated substrates without specifically recognizing the C-terminal carboxy group of the Cys-Gly moiety of gamma-glutamyl compounds or the acceptor molecules [1].
  • A Cys-Gly ... Cys-Gly-X-X-His amino acid pattern was identified in the cysteine-rich protein of CWMV and those of several other plant virus genera, which seems likely to have some functional significance [2].

High impact information on C01419

  • The latter has been characterized and shown to be the principal activity responsible for the hydrolysis of S derivatives of Cys-Gly (including cystinyl-bis-glycine (Cys-bis-Gly) and 5-hydroxy-6-S-cysteinylglycyl-1-7,9-trans-11,14-cis-eicosatetraenoic acid (leukotriene D4)) [3].
  • The enzyme is severalfold more effective in the hydrolysis of dipeptides than aminopeptidase M. Dipeptidase, in contrast to aminopeptidase M, is inhibited by thiol compounds; Cys-Gly, in particular, is a potent inhibitor (Ki = 20 microM) [3].
  • The phi 80 CI repressor was cleaved at a Cys-Gly bond by the wildtype RecA protein in the presence of single-stranded DNA and ATP or its analogues [4].
  • Thus, in the human enzyme, a specific residue in the Cys-Gly binding site played a critical role in recognizing the Cys-Gly moiety or the acceptor molecules by interacting with the C-terminal carboxy group, whereas the Cys side chain and the Cys-Gly amide bond were not recognized significantly [1].
  • The binding site of GGT for the Cys-Gly moiety of glutathione or for the acceptor molecules was probed by the phosphonate diesters to reveal a significant difference in the mechanism of substrate recognition between E. coli and human GGT [1].

Biological context of C01419

  • Its amino acid sequence was shown to be Ala-Cys-Ser-Gly-Arg-Gly-Ser-Arg-Cys-Hyp-Hyp-Gln-Cys-Cys-Met-Gly-Leu-Arg- Cys-Gly - Arg-Gly-Asn-Pro-Gln-Lys-Cys-Ile-Gly-Ala-His-Gla-Asp-Val [5].
  • Removal of Cys-Gly by the kidney depended on Cys-Gly arterial levels and showed a high fractional extraction ( approximately 26%), with clearance rates slightly higher than the glomerular filtration rate (GFR) [6].

Associations of C01419 with other chemical compounds

  • However, purified cystalysin could not catalyze glutathione and Cys-Gly degradation in vitro [7].
  • Although Hcy was released only in low amounts from leg tissues, Cys-Gly (a peptide derived from GSH hydrolysis) was released by both the leg and splanchnic organs, whereas Cys was released by the kidney and taken up by splanchnic organs [6].

Gene context of C01419

  • However, 933W repressor protein contains neither an Ala-Gly nor an alternative Cys-Gly dipeptide cleavage site anywhere in its linker sequence [8].


  1. Design, Synthesis, and Evaluation of gamma-Phosphono Diester Analogues of Glutamate as Highly Potent Inhibitors and Active Site Probes of gamma-Glutamyl Transpeptidase. Han, L., Hiratake, J., Kamiyama, A., Sakata, K. Biochemistry (2007) [Pubmed]
  2. Complete sequence and genome properties of Chinese wheat mosaic virus, a new furovirus from China. Diao, A., Chen, J., Ye, R., Zheng, T., Yu, S., Antoniw, J.F., Adams, M.J. J. Gen. Virol. (1999) [Pubmed]
  3. Glutathione-degrading enzymes of microvillus membranes. Kozak, E.M., Tate, S.S. J. Biol. Chem. (1982) [Pubmed]
  4. Cleavage of bacteriophage phi 80 CI repressor by RecA protein. Eguchi, Y., Ogawa, T., Ogawa, H. J. Mol. Biol. (1988) [Pubmed]
  5. A novel sodium channel inhibitor from Conus geographus: purification, structure, and pharmacological properties. Yanagawa, Y., Abe, T., Satake, M., Odani, S., Suzuki, J., Ishikawa, K. Biochemistry (1988) [Pubmed]
  6. Interorgan exchange of aminothiols in humans. Garibotto, G., Sofia, A., Saffioti, S., Russo, R., Deferrari, G., Rossi, D., Verzola, D., Gandolfo, M.T., Sala, M.R. Am. J. Physiol. Endocrinol. Metab. (2003) [Pubmed]
  7. Role of glutathione metabolism of Treponema denticola in bacterial growth and virulence expression. Chu, L., Dong, Z., Xu, X., Cochran, D.L., Ebersole, J.L. Infect. Immun. (2002) [Pubmed]
  8. Purification and characterization of the repressor of the shiga toxin-encoding bacteriophage 933W: DNA binding, gene regulation, and autocleavage. Koudelka, A.P., Hufnagel, L.A., Koudelka, G.B. J. Bacteriol. (2004) [Pubmed]
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