Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis
Biological Chemistry, ISSN: 1431-6730, Vol: 389, Issue: 9, Page: 1209-1217
2008
- 12Citations
- 9Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations12
- Citation Indexes12
- 12
- CrossRef10
- Captures9
- Readers9
Article Description
The extracellular serine endopeptidase GluSE (EC 3.4.21.19) is considered to be one of the virulence factors of Staphylococcus epidermidis. The present study investigated maturation processing of native GluSE and that heterologously expressed in Escherichia coli. In addition to the 28-kDa mature protease, small amounts of proenzymes with molecular masses of 32, 30, and 29 kDa were identified in the extracellular and cell wall-associated fractions. We defined the pre (M1-A27)- and pro (K28-S66)-segments, and found that processing at the E32-S33 and D48-I49 bonds was responsible for production of the 30- and 29-kDa intermediates, respectively. The full-length form of C-terminally His-tagged GluSE was purified as three proenzymes equivalent to the native ones. These molecules possessing an entire or a part of the pro-segment were proteolytically latent and converted to a mature 28-kDa form by thermolysin cleavage at the S66-V67 bond. Mutation of the essential amino acid S235 suggested auto-proteolytic production of the 30- and 29-kDa intermediates. Furthermore, an undecapeptide (I56-S66) of the truncated pro-segment not only functions as an inhibitor of the protease but also facilitates thermolysin processing. These findings could offer clues to the molecular mechanism involved in the regulation of proteolytic activity of pathogenic proteases secreted from S. epidermidis. © by Walter de Gruyter Berlin New York 2008.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=54049137972&origin=inward; http://dx.doi.org/10.1515/bc.2008.137; http://www.ncbi.nlm.nih.gov/pubmed/18783343; https://www.degruyter.com/view/j/bchm.2008.389.issue-9/bc.2008.137/bc.2008.137.xml; https://www.degruyter.com/view/j/bchm.2008.389.issue-9/bc.2008.137/bc.2008.137.pdf; https://www.degruyter.com/document/doi/10.1515/BC.2008.137/html
Walter de Gruyter GmbH
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