Two C-terminal cysteines are necessary for proper folding of the peptidase neprilysin/CD10

Biochemical and Biophysical Research Communications

Volumn 295, Issue 2, 2002, Pages 423-427

  Santos, Alexander Navarrete ^a   Wulfänger, Jens ^b   Helbing, Grit ^b   Blosz, Tanja ^b   Langner, Jürgen ^b   Riemann, Dagmar ^b  

^a ACGT ProGenomics AG   (Germany)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Caax motif; Disulfide bonds; Green fluorescence protein; Mutagenesis; Neprilysin

Indexed keywords

COMMON ACUTE LYMPHOBLASTIC LEUKEMIA ANTIGEN; MUTANT PROTEIN; PROTEINASE;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CONTROLLED STUDY; ENZYME ACTIVITY; FEMALE; FLOW CYTOMETRY; GENE CONSTRUCT; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; LASER MICROSCOPY; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; SITE DIRECTED MUTAGENESIS; WESTERN BLOTTING; WILD TYPE;

BASE SEQUENCE; CELLS, CULTURED; CYSTEINE; DNA PRIMERS; HUMANS; MUTAGENESIS, SITE-DIRECTED; NEPRILYSIN; PROTEIN FOLDING; PROTEIN ISOPRENYLATION;

EID: 0036065245     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)00675-7     Document Type: Article

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5. CD10
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14. Protein degradation in the endoplasmic reticulum
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16. Conserved cysteine and tryptophan residues of the endothelin-converting enzyme-1 CXAW motif are critical for protein maturation and enzyme activity