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The Burkholderia pseudomallei serine protease MprA is autoproteolytically activated to produce a highly stable enzyme

Paper ID Volume ID Publish Year Pages File Format Full-Text
18303 42717 2007 8 PDF Available
Title
The Burkholderia pseudomallei serine protease MprA is autoproteolytically activated to produce a highly stable enzyme
Abstract

Burkholderia pseudomallei, a tropical pathogen and the causative agent of melioidosis, is known to secrete a serine metalloprotease (MprA) into the internal milieu of the infectious host. This protein has been shown to cause extensive damage to mammalian physiological proteins and its role in the pathogenesis of melioidosis is still under investigation. Previously, we have reported on the epitope mapping of B. pseudomallei protease that revealed a consensus peptide sequence of serine–methionine–alanine (SMA). The serine within this motif is involved in the serine protease catalytic triad and the SMA domain of the B. pseudomallei serine protease could be a major immunodominant domain. We undertook to further characterize the mprA gene and protein to gain deeper insight into the role and mechanism of this protein. Preliminary analysis showed that the crude lysate of expressed recombinant protease was able to hydrolyze gelatin, azocasein and skimmed milk. Further biochemical characterization demonstrated that the expressed protein maintained good proteolytic activity over a wide pH range of 5–11, is stable from 4 °C up to 68 °C and partially digested immunoglobulins A and G, transferrin and myosin. The proteolytic activity was strongly inhibited by phenylmethylsulfonyl fluoride. From our in vitro experimental evidence, we propose a proenzyme processing mechanism similar to that of subtilisin to produce the mature active protease.

Keywords
Serine protease; Burkholderia pseudomallei; Auto-proteolysis
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The Burkholderia pseudomallei serine protease MprA is autoproteolytically activated to produce a highly stable enzyme
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 40, Issue 2, 4 January 2007, Pages 370–377
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us