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Extracellular metalloproteases from bacteria

Abstract

Bacterial extracellular metalloproteases (BEMPs) are a large group of metal-containing proteases secreted by heterotrophic bacteria. In this review, the diversity, structural characteristics, mechanisms of maturation, physiological roles, and applications of BEMPs are described. BEMPs are distributed among nine families of metalloproteases because of differences in primary sequences and structural characteristics. Until now, all of the BEMPs identified have been endoproteases harboring one catalytic Zn2+ in the active centers. BEMPs are usually synthesized as inactive zymogens with a propeptide that is covalently linked to and inhibits the catalytic domain. The removal of the propeptides of BEMPs is dependent on other proteases or an autocleavage process. The main physiological function of BEMPs is to degrade environmental proteins and peptides for bacterial heterotrophic nutrition. As extracellular proteases, BEMPs vary greatly in enzymology properties to adapt to their respective environments. BEMPs have been widely used in the food and pharmaceutical industries. In order to broaden the application of BEMPs, it is essential to explore novel BEMPs and apply gene/protein engineering to improve the production and properties of promising BEMPs.

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Acknowledgments

The work was supported by the National Natural Science Foundation of China (40876072, 31025001, 31070061, and 31000034), the Hi-Tech Research and Development program of China (2006AA09Z414 and SQ2010AA0900521004), the Special Program of China for Marine-scientific Research in the Public Interest (201005032-6), the Natural Science Foundation of Shandong Province, China (JQ200910 and ZR2009DZ002), the Foundation for Young Excellent Scientists in Shandong Province, China (2007BS07007 and BS2010SW015), and Scientific and the Technological Development Program of Shandong Province, China (2010GSF10217).

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Correspondence to Xiu-Lan Chen.

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Wu, J., Chen, X. Extracellular metalloproteases from bacteria. Appl Microbiol Biotechnol 92, 253–262 (2011). https://doi.org/10.1007/s00253-011-3532-8

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Keywords

  • Bacterial extracellular metalloproteases
  • Diversity
  • Structural characteristics
  • Maturation mechanisms
  • Properties
  • Applications