Literature DB >> 10021925

Catalytic activity of carboxypeptidase B and of carboxypeptidase Y with anisylazoformyl substrates.

W L Mock1, D Xu.   

Abstract

Anisylazoformyllysine (CH3OC6H4-N = N-CO-Lys-OH) is rapidly hydrolyzed at the acyl-lysine linkage by the zinc-enzyme porcine carboxypeptidase B. The catalytic reaction is readily monitored spectrophotometrically by disappearance of the intense absorption (348.5 nm, epsilon 18400) of the azo chromophore, which chemically fragments after substrate cleavage. Carboxypeptidase Y has no activity toward this type of substrate.

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Year:  1999        PMID: 10021925     DOI: 10.1016/s0960-894x(98)00715-x

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


  1 in total

1.  Tri-domain bifunctional inhibitor of metallocarboxypeptidases A and serine proteases isolated from marine annelid Sabellastarte magnifica.

Authors:  Maday Alonso-del-Rivero; Sebastian A Trejo; Mey L Reytor; Monica Rodriguez-de-la-Vega; Julieta Delfin; Joaquin Diaz; Yamile González-González; Francesc Canals; Maria Angeles Chavez; Francesc X Aviles
Journal:  J Biol Chem       Date:  2012-03-12       Impact factor: 5.157

  1 in total

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