Engineering the Tat-secretion pathway of Bacillus licheniformis for the secretion of cytoplasmic enzyme arginase
Author:
Funder
National Key Research and Development Program of China
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Biotechnology
Link
https://link.springer.com/content/pdf/10.1007/s00253-023-12917-2.pdf
Reference44 articles.
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2. Anne J, Economou A, Bernaerts K (2017) Protein secretion in gram-positive bacteria: from multiple pathways to biotechnology. Curr Top Microbiol Immunol 404:267–308. https://doi.org/10.1007/82_2016_49
3. Barnett JP, van der Ploeg R, Eijlander RT, Nenninger A, Mendel S, Rozeboom R, Kuipers OP, van Dijl JM, Robinson C (2009) The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements. FASEB J 276(1):232–243. https://doi.org/10.1111/j.1742-4658.2008.06776.x
4. Bewley MC, Jeffrey PD, Patchett ML, Kanyo ZF, Baker EN (1999) Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily. Structure 7(4):435–448. https://doi.org/10.1016/s0969-2126(99)80056-2
5. Bewley MC, Lott JS, Baker EN, Patchett ML (1996) The cloning, expression and crystallisation of a thermostable arginase. FEBS Lett 386(2–3):215–218. https://doi.org/10.1016/0014-5793(96)00459-0
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