Literature DB >> 14741272

Inhibition of alpha-chymotrypsin with thiol-bearing substrate analogues in the presence of zinc ion.

Min Su Han1, Dong Ju Oh, Dong H Kim.   

Abstract

We have demonstrated that thiol-bearing analogues of alpha-chymotrysin (alpha-CT) substrates such as (S)-(1-benzyl-2-thiolethyl)-carbamic acid, benzyl ester (3) inhibits alpha-CT, a prototypical serine protease, in the presence of Zn(II) ion. They constitute a novel class of small molecule inhibitors for alpha-CT believed to inhibit the enzyme by forming a ternary complex consisting of alpha-CT, Zn(II) ion, and the inhibitor.

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Year:  2004        PMID: 14741272     DOI: 10.1016/j.bmcl.2003.11.058

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  1 in total

1.  Noncovalent modification of chymotrypsin surface using an amphiphilic polymer scaffold: implications in modulating protein function.

Authors:  Britto S Sandanaraj; Dharma Rao Vutukuri; Joseph M Simard; Akamol Klaikherd; Rui Hong; Vincent M Rotello; S Thayumanavan
Journal:  J Am Chem Soc       Date:  2005-08-03       Impact factor: 15.419

  1 in total

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