Enzymatic activation of lysine 2,3-aminomutase from Porphyromonas gingivalis.
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.
Brazeau
Brian J
BJ
Biotechnology Development Center-Eddyville, Cargill Incorporated, 1 Cargill Drive, Eddyville, IA 52553, USA. brian_brazeau@cargill.com
Gort
Steven J
SJ
Jessen
Holly J
HJ
Andrew
Amy J
AJ
Liao
Hans H
HH
D002384:Catalysis; D004789:Enzyme Activation; D004926:Escherichia coli / Q000235:genetics; D005288:Ferredoxins / Q000235:genetics / Q000378:metabolism; D005418:Flavodoxin / Q000235:genetics / Q000378:metabolism; D019751:Intramolecular Transferases / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D009247:NADH, NADPH Oxidoreductases / Q000235:genetics / Q000378:metabolism; D016966:Porphyromonas gingivalis / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D005288:Ferredoxins; D005418:Flavodoxin; D011994:Recombinant Proteins; D009247:NADH, NADPH Oxidoreductases; C116041:flavodoxin NADPH oxidoreductase; D019751:Intramolecular Transferases; C021518:lysine 2,3-aminomutase