References
- Zijun, X.; Ping, X. Crit. Rev. Microbiol. 2007, 33, 127. https://doi.org/10.1080/10408410701364604
- McCourt, J. A.; Duggleby, R. G. Amino Acids 2006, 31, 173. https://doi.org/10.1007/s00726-005-0297-3
- Gedi, V.; Yoon, M. Y. FEBS J. 2012, 279, 946. https://doi.org/10.1111/j.1742-4658.2012.08505.x
- Pang, S. S.; Duggleby, R. G.; Schowen, R. L.; Guddat, L. W. J. Biol. Chem. 2004, 279, 2242. https://doi.org/10.1074/jbc.M304038200
- Gedi, V.; Koo, B. S.; Kim, D. E.; Yoon, M. Y. Bull. Korean Chem. Soc. 2010, 31, 3782. https://doi.org/10.5012/bkcs.2010.31.12.3782
- Stormer, F. C. J. Biol. Chem. 1968, 243, 3735.
- Stormer, F. C. J. Biol. Chem. 1968, 243, 3740.
- Holtzclaw, W. D.; Chapman, L. F. J. Bacteriol. 1975, 121, 917.
- Snoep, J. L.; Teixeira de Mattos, M. J.; Starrenburg, M. J. C.; Hugenholtz, J. J. Bacteriol. 1992, 174, 4838.
- Phalip, V.; Schmitt, P.; Divies, C. Curr. Microbiol. 1995, 31, 316. https://doi.org/10.1007/BF00314587
- Peng, H. L.; Wang, P. Y.; Wu, C. M.; Hwang, D. C.; Chang, H. Y. Gene. 1992, 117, 125. https://doi.org/10.1016/0378-1119(92)90500-O
- Shaanan, B.; Chipman, D. M. FEBS J. 2009, 276, 2447. https://doi.org/10.1111/j.1742-4658.2009.06965.x
- Bar-Ilan, A.; Balan, V.; Tittmann, K.; Golbik, R.; Vyazmensky, M.; Hubner, G.; Barak, Z.; Chipman, D. M. Biochemistry 2001, 40, 11946. https://doi.org/10.1021/bi0104524
- Candy, J. M.; Koga, J.; Nixon, P. F.; Duggleby, R. G. Biochem. J. 1996, 315, 745.
- Killenberg-Jabs, M.; Konig, S.; Eberhardt, I.; Hohmann, S.; Hubner, G. Biochemistry 1997, 36, 1900. https://doi.org/10.1021/bi961341l
- Lee, S. C.; Kim, J.; La, I. J.; Kim, S. K.; Yoon, M. Y. Enzyme Microb. Technol. 2013, 52, 54. https://doi.org/10.1016/j.enzmictec.2012.10.006
- La, I. J.; Karim, M.; Yoon, M. Y. Bull. Korean Chem. Soc. 2008, 29(9), 1823. https://doi.org/10.5012/bkcs.2008.29.9.1823
- Dobritzsch, D.; Konig, S.; Schneider, G.; Lu, G. J. Biol. Chem. 1998, 273, 20196. https://doi.org/10.1074/jbc.273.32.20196
- Pang, S. S.; Duggleby, R. G.; Guddat, L. W. J. Mol. Biol. 2002, 317, 249. https://doi.org/10.1006/jmbi.2001.5419
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