Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0378-1119(02)01151-4
Title: Cloning and characterization of a metalloprotease from Vibrio harveyi strain AP6
Authors: Teo, J.W.P.
Poh, C.L. 
Zhang, L.-H. 
Keywords: Pathogenesis
Zinc metalloprotease
Zinc-binding motif
Issue Date: 2003
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.
Source Title: Gene
URI: http://scholarbank.nus.edu.sg/handle/10635/31475
ISSN: 03781119
DOI: 10.1016/S0378-1119(02)01151-4
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