Bacterial production of D-erythroascorbic acid and L-ascorbic acid through functional expression of Saccharomyces cerevisiae D-arabinono-1,4-lactone oxidase in Escherichia coli.
D-Arabinono-1,4-lactone oxidase, which catalyzes the terminal step in the biosynthesis of D-erythroascorbic acid in Saccharomyces cerevisiae, was functionally expressed in Escherichia coli inherently lacking the enzyme. The recombinant E. coli strain expressing the enzyme could overproduce D-erythroascorbic acid and L-ascorbic acid when supplied with D-arabinono-1,4-lactone and L-galactono-1,4-lactone, respectively.
Lee
B H
BH
Laboratory of Biophysics, Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University, Seoul 151-742, Republic of Korea.
Huh
W K
WK
Kim
S T
ST
Lee
J S
JS
Kang
S O
SO
D001205:Ascorbic Acid / Q000096:biosynthesis*; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013401:Sugar Alcohol Dehydrogenases / Q000096:biosynthesis*
D011994:Recombinant Proteins; C005056:isoascorbic acid; D013401:Sugar Alcohol Dehydrogenases; C090492:D-arabinonolactone oxidase; D001205:Ascorbic Acid