Enzymatic Activation of Lysine 2,3-Aminomutase from Porphyromonas gingivalis
- 1 September 2006
- journal article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 72 (9) , 6402-6404
- https://doi.org/10.1128/aem.01143-06
Abstract
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.Keywords
This publication has 19 references indexed in Scilit:
- Trends and innovations in industrial biocatalysis for the production of fine chemicalsCurrent Opinion in Biotechnology, 2004
- Dispelling the Myths--Biocatalysis in Industrial SynthesisScience, 2003
- Radical Mechanisms of Enzymatic CatalysisAnnual Review of Biochemistry, 2001
- Direct FeS Cluster Involvement in Generation of a Radical in Lysine 2,3-AminomutaseBiochemistry, 2000
- Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotidesPublished by Elsevier ,1999
- Escherichia coliBiotin Synthase: An Investigation into the Factors Required for Its Activity and Its Sulfur DonorArchives of Biochemistry and Biophysics, 1996
- An organic radical in the lysine 2,3-aminomutase reactionBiochemistry, 1992
- Routes of Flavodoxin and Ferredoxin Reduction in Escherichia coliEuropean Journal of Biochemistry, 1982
- [40] Ferredoxin-NADP reductase from spinachPublished by Elsevier ,1971
- Flavodoxin and Ferredoxm ofEscherichia coliHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1971