Literature DB >> 7811266

Guinea pig membrane-bound aminopeptidase P is a member of the proline peptidase family.

N D Denslow1, J W Ryan, H P Nguyen.   

Abstract

Members of the newly recognized proline peptidase family share the ability to hydrolyze imide bonds and share six blocks of highly homologous amino acid sequences. We have found that guinea pig lung and kidney forms of aminopeptidase P, both forms bound to membranes via glycosyl phosphatidylinositol lipid anchors, share at least three of the six conserved blocks of amino acid sequences. In addition, aminopeptidase P acts as an aminoacylproline hydrolase and thus appears to be a member of the proline peptidase family.

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Year:  1994        PMID: 7811266     DOI: 10.1006/bbrc.1994.2877

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


  2 in total

1.  Molecular cloning and expression in COS-1 cells of pig kidney aminopeptidase P.

Authors:  R J Hyde; N M Hooper; A J Turner
Journal:  Biochem J       Date:  1996-10-01       Impact factor: 3.857

2.  Human recombinant membrane-bound aminopeptidase P: production of a soluble form and characterization using novel, internally quenched fluorescent substrates.

Authors:  Giuseppe Molinaro; Adriana K Carmona; Maria A Juliano; Luiz Juliano; Elena Malitskaya; Marie-Andrée Yessine; Miguel Chagnon; Yves Lepage; William H Simmons; Guy Boileau; Albert Adam
Journal:  Biochem J       Date:  2005-01-15       Impact factor: 3.857

  2 in total

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