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Chemical Compound Review:

CHEMBL560871 2-[2- (diaminomethylideneamino) ethylsulfany...

Synonyms: AG-K-77039, CHEBI:655474, AC1L1FZW, AC1Q5SXD, CTK5E4534, ...

Powell, A.M. et al., Song, L. et al., Qian, Y. et al., Deddish, P.A. et al., Rossier, J. et al., et al.

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High impact information on guanidinoethylmercaptosuccinic acid

Enkephalin convertase, an enkephalin-forming carboxypeptidase, is potently inhibited by guanidinoethylmercaptosuccinic acid (GEMSA) [1].
Wild-type CPE and the Gln300 point mutant bound to a p-aminobenzoyl-Arg-Sepharose affinity resin, and this binding was competed by an active site-directed inhibitor, guanidinoethylmercaptosuccinic acid [2].
Several active site-directed inhibitors also show generally similar potency toward the two enzymes, although guanidinoethylmercaptosuccinic acid is approximately 10-fold more potent, and hippuryl-Arg is approximately 100-fold more potent as an inhibitor of CPD than of CPE [3].
5. Guanidinoethylmercaptosuccinic acid inhibited the membrane-bound carboxypeptidase M more effectively than the purified enzyme, and the IC50 was about 25-30 times lower at pH 5 [4].
In every case 25 microM guanidinoethylmercaptosuccinic acid, an active site-directed inhibitor of carboxypeptidase H, completely inhibits the activity [5].

Anatomical context of guanidinoethylmercaptosuccinic acid

Incubation of unfixed, frozen sections of rat pancreas with tritiated guanidinoethylmercaptosuccinic acid (GEMSA) resulted in a localization of [3H]-GEMSA autoradiographic grains over the islets of Langerhans, suggesting that a carboxypeptidase H-like enzyme occurs in the islet [6].

References

Enkephalin convertase localization by [3H]guanidinoethylmercaptosuccinic acid autoradiography: selective association with enkephalin-containing neurons. Lynch, D.R., Strittmatter, S.M., Snyder, S.H. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway. Qian, Y., Varlamov, O., Fricker, L.D. J. Biol. Chem. (1999) [Pubmed]
Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary. Song, L., Fricker, L.D. J. Biol. Chem. (1995) [Pubmed]
Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase). Deddish, P.A., Skidgel, R.A., Erdös, E.G. Biochem. J. (1989) [Pubmed]
Radiometric assay for carboxypeptidase H (EC 3.4.17.10) and other carboxypeptidase B-like enzymes. Rossier, J., Barrès, E., Hutton, J.C., Bicknell, R.J. Anal. Biochem. (1989) [Pubmed]
Autoradiographic localization of [3H]-guanidinoethylmercaptosuccinic acid binding sites in rat islets of Langerhans. Powell, A.M., Wells, M.R., Timmers, K.I., Recant, L. Life Sci. (1987) [Pubmed]

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