ライフサイエンスコーパス: enteropeptidase

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1 on trypsinogen activation catalyzed by human enteropeptidase.

2 fic substrate for human, but not for bovine, enteropeptidase.

3 Enteropeptidase, a type II transmembrane protein of the

4 Enteropeptidase, also known as enterokinase, initiates t

5 Thus enteropeptidase appears to have at least three distinct

6 e solved the crystal structure of the bovine enteropeptidase catalytic domain to 2.3 A resolution in

7 In this location, enteropeptidase cleaves and activates trypsinogen, there

8 as a single-chain protein, whereas purified enteropeptidase contains a approximately 47-kDa serine p

9 These results suggest apical sorting of enteropeptidase depends on N-linked glycosylation of the

10 contrast to many apically targeted proteins, enteropeptidase does not form detergent-resistant associ

11 inogen was activated efficiently by purified enteropeptidase from bovine intestine (Km = 5.6 microM a

12 These kinetic data indicate that the enteropeptidase heavy chain has little influence on the

13 Enteropeptidase is a heterodimeric type II membrane prot

14 Enteropeptidase is a membrane-bound serine protease that

15 Enteropeptidase is synthesized as a single-chain protein

16 ty of two unrelated proteases, caspase-3 and enteropeptidase (or enterokinase).

17 light chain (pro-HL-BEK (where BEK is bovine enteropeptidase)) or only the catalytic domain (pro-L-BE

18 Asp(19-22) motif per se is not required for enteropeptidase recognition, whereas it is essential for

19 Treatment of conditioned medium with enteropeptidase reduced the apparent molecular mass of t

20 Thus, a unique basic exosite on the enteropeptidase surface has evolved to facilitate the cl

21 dic motif as a specific recognition site for enteropeptidase, the physiological activator of trypsino

22 Recombinant bovine enteropeptidase was sorted directly to the apical surfac

23 Enteropeptidase was unexpectedly promiscuous, but exhibi

24 ed mRNA encoding PAR(2), trypsinogen IV, and enteropeptidase, which activates the zymogen.

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