In:
FEBS Letters, Wiley, Vol. 426, No. 1 ( 1998-04-10), p. 41-46
Abstract:
Recent studies have demonstrated that a serpin variant, α 1 ‐antitrypsin Portland (AT‐PDX), can inhibit the mammalian convertase furin. Here, we examine the mechanism by which this inhibition takes place. We find that furin, which does not belong to the trypsin‐like serine protease family, the usual targets of serpins, forms an SDS‐heat denaturation‐resistant complex with AT‐PDX both in vitro and in vivo. AT‐PDX inhibited furin with an association rate constant ( k ass ) of 1.5×10 6 M −1 s −1 which is similar to k ass values reported for serpins with trypsin‐like enzymes. These results illustrate that AT can be modified to act essentially as a suicide inhibitor of furin, an enzyme of the subtilase superfamily of serine proteases.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(98)00307-X
Language:
English
Publisher:
Wiley
Publication Date:
1998
detail.hit.zdb_id:
1460391-3
SSG:
12