Glycosylation of Asn-632 and Asn-651 is important for functional expression of endothelin-converting enzyme-1.
It has been shown previously that N-glycosylation of Asn-144 and/or Asn-627 is important for functional expression of neutral endopeptidase-24.11 (NEP). All glycosylation sites of NEP are conserved within endothelin-converting enzyme-1 (ECE-1). In the present study we investigated the importance of proper glycosylation for the biologic function of ECE-1. We show that the double mutation of Asn-632 and Asn-651 leads to expression of an enzymatically inactive ECE-1 protein. In contrast, the single mutation of either Asn-632 or Asn-651 did not alter the enzymatic activity of ECE-1b.
Nelboeck
P
P
F. Hoffmann-La Roche Ltd., Pharma Division, Preclinical Research, Basel, Switzerland.
Fuchs
M
M
Bur
D
D
Löffler
B M
BM
D000818:Animals; D001216:Asparagine / Q000235:genetics / Q000378:metabolism*; D016282:Aspartic Acid Endopeptidases / Q000096:biosynthesis* / Q000235:genetics; D015153:Blotting, Western; D016466:CHO Cells; D006224:Cricetinae; D000072396:Endothelin-Converting Enzymes; D006031:Glycosylation; D008666:Metalloendopeptidases / Q000096:biosynthesis* / Q000235:genetics; D009154:Mutation; D014176:Protein Biosynthesis
D001216:Asparagine; D016282:Aspartic Acid Endopeptidases; D008666:Metalloendopeptidases; D000072396:Endothelin-Converting Enzymes