The FAXWXXT motif in the carboxyl terminus of Vibrio mimicus metalloprotease is involved in binding to collagen.
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.
Lee
Jong-Hee
JH
Department of Biotechnology and Bioengineering, Pukyong National University, Busan, Republic of Korea.
Ahn
Sun-Hee
SH
Lee
Eun-Mi
EM
Jeong
Seung-Ha
SH
Kim
Young-Ok
YO
Lee
Sang-Jun
SJ
Kong
In-Soo
IS
D020816:Amino Acid Motifs; D003094:Collagen / Q000378:metabolism*; D007700:Kinetics; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D016415:Sequence Alignment; D044164:Vibrio mimicus / Q000201:enzymology*
D010446:Peptide Fragments; D011994:Recombinant Proteins; D003094:Collagen; D008666:Metalloendopeptidases