The ultimate tryptophan residue of neprilysin 2 is not involved in protein maturation and enzymatic activity

Biochemical and Biophysical Research Communications

Volumn 335, Issue 2, 2005, Pages 356-360

  Voisin, Stéphanie ^a   Ouimet, Tanja ^a  

^a CENTRE PAUL BROCA   (France)

Author keywords

Endothelin converting enzyme 1; M13 family; Metalloproteases; Neprilysin; Neprilysin 2; Site directed mutagenesis

Indexed keywords

AMINO ACID; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE; PROLINE; TRYPTOPHAN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; MOUSE; MUTAGENESIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN SECRETION; PROTEIN STRUCTURE; RAT;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATALYSIS; CELL LINE; CELL LINE, TUMOR; GENE DELETION; HYDROLYSIS; IMMUNOBLOTTING; KINETICS; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; NEPRILYSIN; PEPTIDES; PROLINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TRYPTOPHAN;

EID: 23744489121     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.07.081     Document Type: Article

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