Literature DB >> 6552186

A Met-enkephalin-containing-peptide, BAM 22P, as a novel substrate for glandular kallikreins.

E S Prado, L Prado de Carvalho, M S Araujo-Viel, N Ling, J Rossier.   

Abstract

Homogeneous preparations of two well-characterized glandular kallikreins have been examined for their ability to hydrolyze BAM 22P, a methionine-enkephalin-containing-peptide found in the adrenal medulla. Both enzymes cleaved preferentially the Arg6-Arg7 bond in this substrate. The specificity constant (kcat/Km) for this cleavage was 86 mM-1 sec-1 for horse urinary kallikrein and 566 mM-1 sec-1 for porcine pancreatic kallikrein. These results demonstrate a previously undescribed specificity for glandular kallikreins and suggest a possible role for these widely distributed enzymes in prohormone processing.

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Year:  1983        PMID: 6552186     DOI: 10.1016/0006-291x(83)91472-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Specificity of human tissue kallikrein towards substrates containing Phe-Phe pair of amino acids.

Authors:  D C Pimenta; J Chao; L Chao; M A Juliano; L Juliano
Journal:  Biochem J       Date:  1999-04-15       Impact factor: 3.857

2.  Evaluation of the extent of the binding site in human tissue kallikrein by synthetic substrates with sequences of human kininogen fragments.

Authors:  E Del Nery; J R Chagas; M A Juliano; E S Prado; L Juliano
Journal:  Biochem J       Date:  1995-11-15       Impact factor: 3.857

3.  Determinants of the unusual cleavage specificity of lysyl-bradykinin-releasing kallikreins.

Authors:  J R Chagas; F C Portaro; I Y Hirata; P C Almeida; M A Juliano; L Juliano; E S Prado
Journal:  Biochem J       Date:  1995-02-15       Impact factor: 3.857

  3 in total

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