Enzymatic activation of lysine 2,3-aminomutase from Porphyromonas gingivalis.

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.

SUBMITTER: Brazeau BJ 

PROVIDER: S-EPMC1563663 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature