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Enzymology and Protein Engineering

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

Brian J. Brazeau, Steven J. Gort, Holly J. Jessen, Amy J. Andrew, Hans H. Liao
Brian J. Brazeau
1Biotechnology Development Center—Eddyville, Cargill Incorporated, 1 Cargill Drive, Eddyville, Iowa
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  • For correspondence: brian_brazeau@cargill.com
Steven J. Gort
2Biotechnology Development Center, Cargill Incorporated, 2500 Shadywood Road, Navarre, Minnesota
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Holly J. Jessen
2Biotechnology Development Center, Cargill Incorporated, 2500 Shadywood Road, Navarre, Minnesota
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Amy J. Andrew
3Department of Biochemistry, University of Wisconsin—Madison, Madison, Wisconsin
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Hans H. Liao
2Biotechnology Development Center, Cargill Incorporated, 2500 Shadywood Road, Navarre, Minnesota
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DOI: 10.1128/AEM.01143-06
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    FIG. 1.

    Effect of electron transfer proteins on activity of KAMPg. (A) A 100 μM concentration of FPR (solid line, solid circles), FLD (dashed line, solid circles), or FD (dotted line, solid circles) was added individually to as-isolated KAMPg. The data for KAMPg with no electron transfer protein added is also shown (solid line, open circles). (B) A 100 μM concentration of FLD (dashed line, open circles), FPR (dotted line, solid circles), or 100 μM FLD plus 100 μM FPR (solid line, solid circles) was added to as-isolated KAMPg. (C) A 100 μM concentration of FD (dashed line, solid circles), FPR (dotted line, solid circles), or 100 μM FD plus 100 μM FPR (solid line, solid circles) was added to as-isolated KAMPg. The inset shows an overlay of 100 μM FLD plus 100 μM FPR and 100 μM FD plus 100 μM FPR. Each assay was performed as described in the text and was repeated at least three times. The lines through the data points do not represent the fit of a kinetic model; they are included only for clarity.

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    FIG. 2.

    The activity of KAMPg is dependent upon the concentration of each electron transfer protein. Various concentrations of FPR (A), FD (B), and FLD (C) were used. The concentration of KAMPg was 5 μM. All assays were performed as described in the text and were repeated at least three times. The lines through the data points do not represent the fit of a kinetic model; they are included only for clarity.

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Enzymatic Activation of Lysine 2,3-Aminomutase from Porphyromonas gingivalis
Brian J. Brazeau, Steven J. Gort, Holly J. Jessen, Amy J. Andrew, Hans H. Liao
Applied and Environmental Microbiology Sep 2006, 72 (9) 6402-6404; DOI: 10.1128/AEM.01143-06

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Enzymatic Activation of Lysine 2,3-Aminomutase from Porphyromonas gingivalis
Brian J. Brazeau, Steven J. Gort, Holly J. Jessen, Amy J. Andrew, Hans H. Liao
Applied and Environmental Microbiology Sep 2006, 72 (9) 6402-6404; DOI: 10.1128/AEM.01143-06
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KEYWORDS

Intramolecular Transferases
Porphyromonas gingivalis

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