Please use this identifier to cite or link to this item:
|Title:||Cloning and characterization of a metalloprotease from Vibrio harveyi strain AP6|
|Source:||Teo, J.W.P.,Poh, C.L.,Zhang, L.-H. (2003). Cloning and characterization of a metalloprotease from Vibrio harveyi strain AP6. Gene 303 (1-2) : 147-156. ScholarBank@NUS Repository. https://doi.org/10.1016/S0378-1119(02)01151-4|
|Abstract:||A metalloprotease gene pap6 was cloned from Vibrio harveyi strain AP6. Sequence analysis showed that pap6 was 2034 bp in length and predicted to encode a peptide of 677 amino acids with a molecular mass of 75 kDa. SDS-PAGE analysis of the purified Pap6 revealed that it was 35 kDa in size. N-terminal amino acid sequencing established that the mature protein began at Leu-191, suggesting that the preprotein of Pap6 was processed to generate a mature protease. Purified Pap6 was characterized as a zinc metalloprotease as it was inhibited by zinc- and metal-specific inhibitors such as 1, 10-phenanthroline, EGTA and EDTA. The deduced amino acid sequence revealed the presence of a zinc-binding motif HEXXH∼19aa∼E. Substitution of these active site residues by site-directed mutagenesis caused significant losses in enzyme activity, thus demonstrating their involvement in catalysis. Pap6 was shown to digest a range of host proteins, including gelatin, fibronectin, and type IV collagen, indicating a potential role in pathogenesis. © 2002 Elsevier Science B.V. All rights reserved.|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Dec 5, 2017
WEB OF SCIENCETM
checked on Nov 3, 2017
checked on Dec 9, 2017
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.