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|Title:||Cloning and characterization of a metalloprotease from Vibrio harveyi strain AP6|
|Citation:||Teo, J.W.P., Zhang, L.-H., Poh, C.L. (2003-01-16). 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|
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