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Applied and Environmental Microbiology, September 2006, p. 6402-6404, Vol. 72, No. 9
0099-2240/06/$08.00+0     doi:10.1128/AEM.01143-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Enzymatic Activation of Lysine 2,3-Aminomutase from Porphyromonas gingivalis

Brian J. Brazeau,1* Steven J. Gort,2 Holly J. Jessen,2 Amy J. Andrew,3 and Hans H. Liao2

Biotechnology Development Center—Eddyville, Cargill Incorporated, 1 Cargill Drive, Eddyville, Iowa,1 Biotechnology Development Center, Cargill Incorporated, 2500 Shadywood Road, Navarre, Minnesota,2 Department of Biochemistry, University of Wisconsin—Madison, Madison, Wisconsin3

Received 17 May 2006/ Accepted 18 June 2006

The development of lysine 2,3-aminomutase as a robust biocatalyst hinges on the development of an in vivo activation system to trigger catalysis. This is the first report to show that, in the absence of chemical reductants, lysine 2,3-aminomutase activity is dependent upon the presence of flavodoxin, ferredoxin, or flavodoxin-NADP+ reductase.

* Corresponding author. Mailing address: Biotechnology Development Center—Eddyville, Cargill Incorporated, 1 Cargill Drive, Eddyville, IA 52553. Phone: (641) 969-7045. Fax: (641) 969-3850. E-mail: brian_brazeau{at}cargill.com.

Applied and Environmental Microbiology, September 2006, p. 6402-6404, Vol. 72, No. 9
0099-2240/06/$08.00+0     doi:10.1128/AEM.01143-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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