Premium
The FAXWXXT motif in the carboxyl terminus of Vibrio mimicus metalloprotease is involved in binding to collagen
Author(s) -
Lee Jong-Hee,
Ahn Sun-Hee,
Lee Eun-Mi,
Jeong Seung-Ha,
Kim Young-Ok,
Lee Sang-Jun,
Kong In-Soo
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.062
Subject(s) - collagenase , metalloproteinase , amino acid , peptide , biochemistry , chemistry , n terminus , peptide sequence , extracellular , c terminus , vibrio , enzyme , biology , microbiology and biotechnology , bacteria , gene , genetics
We have shown previously that the C‐terminal region of the extracellular metalloprotease of Vibrio mimicus (VMC) is essential for collagenase activity. Here, we demonstrate that deletion of 100 amino acids, but not 67 amino acids, from the C‐terminus of the intact VMC protein (VMC61) abolished the collagenase activity. The intervening 33‐amino acid region contains a repeated FAXWXXT motif that is essential for insoluble type I collagen binding; the isolated 33‐amino acid peptide bound to insoluble type I collagen, while a peptide containing only the first FAXWXXT motif did not. Compared to the VMC61, the 33‐amino acid peptide corresponding to the C‐terminus exhibited a similar binding affinity and a lower binding capacity.