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Chemical Compound Review

Llvy-mca     3-[[1-[[1-[[(1S)-1-[[(1S)-2- (4...

Synonyms: Sllvt-mca, Suc-llvy-mca, AR-1J8461, AC1L3TL1, AC1Q5VQ9, ...
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Disease relevance of Suc-leu-leu-val-tyr-mca

  • Succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide (Suc-LLVY-MCA) hydrolyzing activities of the 20S and 26S proteasomes in the gerbil cortex following transient forebrain ischemia were examined [1].

High impact information on Suc-leu-leu-val-tyr-mca

  • IFN-gamma stimulation results in a downregulation of the chymotrypsin-like Suc-LLVY-MCA peptide hydrolyzing activity of 20S proteasomes whereas the trypsin-like activity remains unaffected [2].
  • After hydrogen peroxide treatment of K562 cells, degradation of the model proteasome peptide substrate suc-LLVY-MCA and degradation of oxidized histones in nuclei increases significantly within minutes [3].
  • In vitro, the 20S proteasome shows an increased proteolytic activity toward oxidized polypeptides and the suc-LLVY-MCA peptide specific for its chymotrypsin-like activity [4].
  • Proteasomes eluted in the other peak were partially resolved into three subpeaks and based on their preferential hydrolysis of casein, Z-GGL-MCA, and suc-LLVY-MCA, were designated C, L and Y, respectively [5].
  • The three fatty acids all activated the hydrolysis of succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide (Suc-LLVY-MCA) and benzyloxycarbonyl-Leu-Leu-Glu-2-naphthyl-amide (Cbz-LLE-2NA) at low concentrations (one-third to one-sixth of that required for activation by SDS) [6].

Biological context of Suc-leu-leu-val-tyr-mca

  • Suc-LLVY-MCA degrading activity of the platelet proteasome showed positive cooperativity between two or more catalytic sites because the coefficient was 1.54 when analyzed by use of the Hill plot [7].

Anatomical context of Suc-leu-leu-val-tyr-mca

  • The egg jelly-induced acrosome reaction of the sea urchin, Strongylocentrotus intermedius, was inhibited by succinyl-Leu-Leu-Val-Tyr-4-methyl-coumaryl-7-amide (Suc-Leu-Leu-Val-Tyr-MCA), but not by Suc-Ala-Ala-Pro-Phe-MCA [8].
  • To characterize a chymotrypsin-like hydrolytic activity in the cell surface membranes of intact opossum kidney (OK) cells, we partially purified a protease from the membrane fractions of OK cells using Suc-Leu-Leu-Val-Tyr-MCA (Suc, succinyl; MCA, 4-methylcoumaryl-7-amide), a synthetic substrate for chymotrypsin, as the substrate [9].
  • The localization of the proteolytic activity was tested by fractionation of the compartments of rat liver mitochondria using the flourogenic peptide suc-Leu-Leu-Val-Tyr-MCA as substrate [10].

Associations of Suc-leu-leu-val-tyr-mca with other chemical compounds


Gene context of Suc-leu-leu-val-tyr-mca

  • Using Suc-Leu-Leu-Val-Tyr-MCA, a specific substrate for PA protease, M1 was demonstrated to inhibit the amidolytic activity of PA, whereas M1 did not inhibit that of chymotrypsin or trypsin at all [11].
  • Thus, while calpain was inhibited by similar concentrations of ZLLal and ZLLLal, the inhibitory potencies of ZLLLal against the ZLLL-MCA- and Suc-LLVY-MCA-degrading activities in proteasome were 1,100 and 140 times stronger than those of ZLLal, respectively [12].


  1. Changes in proteasome activity following transient ischemia. Kamikubo, T., Hayashi, T. Neurochem. Int. (1996) [Pubmed]
  2. Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. Boes, B., Hengel, H., Ruppert, T., Multhaup, G., Koszinowski, U.H., Kloetzel, P.M. J. Exp. Med. (1994) [Pubmed]
  3. Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones. Ullrich, O., Reinheckel, T., Sitte, N., Hass, R., Grune, T., Davies, K.J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  4. Modulation of the chymotrypsin-like activity of the 20S proteasome by intracellular redox status: effects of glutathione peroxidase-1 overexpression and antioxidant drugs. Kretz-Remy, C., Arrigo, A.P. Biol. Chem. (2003) [Pubmed]
  5. Screening for molecules interacting with proteasomes in Thermoplasma acidophilum. Ehlers, C., Kopp, F., Dahlmann, B. Biol. Chem. (1997) [Pubmed]
  6. Activation of 20S proteasomes from spinach leaves by fatty acids. Watanabe, N., Yamada, S. Plant Cell Physiol. (1996) [Pubmed]
  7. Purification and characterization of endogenous protein activator of human platelet proteasome. Yukawa, M., Sakon, M., Kambayashi, J., Shiba, E., Kawasaki, T., Uemura, Y., Murata, K., Tanaka, T., Nakayama, T., Shibata, H. J. Biochem. (1993) [Pubmed]
  8. Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction. Matsumura, K., Aketa, K. Mol. Reprod. Dev. (1991) [Pubmed]
  9. Characterization of a chymotrypsin-like hydrolytic activity in the opossum kidney cell. Arao, M., Yamaguchi, T., Sugimoto, T., Fukase, M., Chihara, K. Biochem. Cell Biol. (1994) [Pubmed]
  10. Identification of a novel ATP-dependent proteolytic activity in mitochondrial intermembrane space. Sitte, N., Drung, I., Dubiel, W. Biochem. Mol. Biol. Int. (1995) [Pubmed]
  11. Inhibition of the protease activity of influenza virus RNA polymerase PA subunit by viral matrix protein. Hara, K., Shiota, M., Kido, H., Watanabe, K., Nagata, K., Toyoda, T. Microbiol. Immunol. (2003) [Pubmed]
  12. Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine. Tsubuki, S., Saito, Y., Tomioka, M., Ito, H., Kawashima, S. J. Biochem. (1996) [Pubmed]
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