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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Catalysis
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Enzyme Activation
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Escherichia coli / genetics
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Ferredoxins / genetics
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Ferredoxins / metabolism
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Flavodoxin / genetics
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Flavodoxin / metabolism
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Intramolecular Transferases / genetics
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Intramolecular Transferases / metabolism*
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Kinetics
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NADH, NADPH Oxidoreductases / genetics
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NADH, NADPH Oxidoreductases / metabolism
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Porphyromonas gingivalis / enzymology*
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Porphyromonas gingivalis / genetics
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
Substances
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Ferredoxins
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Flavodoxin
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Recombinant Proteins
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NADH, NADPH Oxidoreductases
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flavodoxin NADPH oxidoreductase
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Intramolecular Transferases
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lysine 2,3-aminomutase