Mutation in the substrate-binding site of aminopeptidase B confers new enzymatic properties

Author:

Pham Viet-Laï,Gouzy-Darmon Cécile,Pernier Julien,Hanquez Chantal,Hook Vivian,Beinfeld Margery C.,Nicolas Pierre,Etchebest Catherine,Foulon Thierry,Cadel Sandrine

Publisher

Elsevier BV

Subject

General Medicine,Biochemistry

Reference54 articles.

1. Isolation and characterization of a dibasic selective metalloendopeptidase from rat testis that cleaves at the aminoterminus of arginine residues;Chesneau;J. Biol. Chem.,1994

2. Unique cleavage specificity of “prohormone thiol protease” related to proenkephalin processing;Azaryan;FEBS Lett.,1994

3. Aminopeptidase-B in the rat testis: isolation, functional properties and cellular localization in the seminiferous tubules;Cadel;Mol. Cell. Endocrinol.,1995

4. NRD convertase and Aminopeptidase B: two putative processing metallopeptidases with a selectivity for basic residues;Foulon;Ann. Endocrinol.,1997

5. Aminopeptidase B: from protein to gene;Cadel;Curr. Top. Pept. Prot. Res.,2004

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