Identification and characterization of human polyserase-3, a novel protein with tandem serine-protease domains in the same polypeptide chain.

ABSTRACT:

Background

We have previously described the identification and characterization of polyserase-1 and polyserase-2, two human serine proteases containing three different catalytic domains within the same polypeptide chain. Polyserase-1 shows a complex organization and it is synthesized as a membrane-bound protein which can generate three independent serine protease domains as a consequence of post-translational processing events. The two first domains are enzymatically active. By contrast, polyserase-2 is an extracellular glycosylated protein whose three protease domains remain embedded in the same chain, and only the first domain possesses catalytic activity.

Results

Following our interest in the study of the human degradome, we have cloned a human liver cDNA encoding polyser

SUBMITTER: Cal S 

PROVIDER: S-EPMC1435904 | biostudies-literature | 2006 Mar

REPOSITORIES: biostudies-literature