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Magnetic Resonance Team, Korea Basic Science Institute (KBSI), Ochang, Chungbuk 363-883, KoreaReceived June 26, 2012, Accepted July 6, 2012Vibrio extracellular metalloprotease (vEP), secreted from Vibrio vulnificus , shows various proteolytic functionsuch as prothrombin activation and fibrinolytic activities. Premature form of vEP has an N-terminal (nPP) anda C-terminal (C-ter100) re gion. The nPP and C-ter100 regions are autocl eaved for the matu red metalloproteaseactivity. It has been proposed that two regions play a key role in regulating enzymatic activity of vEP.Especially, C-ter100 has a regulatory function on proteolytic activity of vEP. C-ter100 domain has been clonedinto the E. coli expression vectors, pET32a and pG EX 4T-1 with TEV pr otease cleav age site and pu rified usinggel-filtration chromatography followed by affinity chromatography. To understand how C-ter100 modulatesproteolytic activity of vEP, structural studies were performed by heteronuclar multi-dimensional NMRspectroscopy. Backbone

bulletin of the korean chemical society

1H,15N and13C Backbone Assignments and Secondary Structures of C-ter100 Domain of Vibrio Extracellular Metalloprotease Derived from Vibrio vulnificus