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Kim, Hak-Jung
- BMB Reports
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- v.39 no.2
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- pp.223-227
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- 2006
Dihydrolipoamide dehydrogenase (E3) belongs to the pyridine nucleotide-disulfide oxidoreductase family including glutathione reductase and thioredoxin reductase. It catalyzes the reoxidation of dihydrolipoyl moiety of the acyltransferase components of three $\alpha$-keto acid dehydrogenase complexes and of the hydrogen-carrier protein of the glycine cleavage system. Isoleucine-51 of human E3, located near the active disulfide center Cys residues, is highly conserved in most E3s from several sources. To examine the importance of this highly conserved Ile-51 in human E3 function, it was substituted with Ala using site-directed mutagenesis. The mutant was expressed in Escherichia coli and highly purified using an affinity column. Its E3 activity was decreased about 100-fold, indicating that the conservation of the Ile-51 residue in human E3 was very important to the efficient catalytic function of the enzyme. Its altered spectroscopic properties implied that conformational changes could occur in the mutant.
https://doi.org/10.5483/BMBRep.2006.39.2.223 인용 PDF

최도진;김원극전억한
- KSBB Journal
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- v.5 no.3
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- pp.223-227
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- 1990
This study describes the sorbitol production with permeabilized cells of Zymomonas mobilis immobilized in Ca-alginate. Toluene treated cells lose glucose-fructose oxidoreductase activity due to leaking of enzyme from the cells. In order to prevent this leakage, the permeabilized cells were immobilized in alginate and chitin. No significant loss of enzyme activity was apparent during 210h operation in a continuous process. The productivity of the continuous process was estimated to be about 3.5g/l -h for sorbitol at dilution rate $0.2h^{-1}$.
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Koh, Young-Sang;Choih, Jenny;Roe, Jung-Hye
- Journal of Microbiology
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- v.34 no.2
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- pp.137-143
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- 1996
We isolated a promoter inducible by paraquat, a superoxide-generating agent, from Escherichia coli using a promoter-probing plasmid pRS415. From sequence analysis we found out the promoter is for fpr ENCODING nadph : ferredoxin oxidoreductase. We constructed on operon fusion of lacZ gene with fpr promoter to monitor the expression of the gene in the single-copy state. LacZ expression generators, menadione and plumbagin, also induced the expression of .betha.-galactosidase in the fusion strain. On the other hand, no significant induction was observed by treatment with hydrogen peroxide, ethanol, and heat shock. Induction of .betha.-galactosidase was significantly reduced by introducing a .DELTA. sox 8 :: cat of soxS3 :: Tn10 mutation into the fusion strain, indicating that fpr gene is a member of the soxRS regulon. The transcriptional start site was determined by primer extension analysis. Possible roles of fpr induction in superoxide stress were discussed.
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JEON SUNG JIN;SHIN IN HO;SANG BYUNG IN;PARK DOO HYUN
- Journal of Microbiology and Biotechnology
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- v.15 no.2
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- pp.281-286
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- 2005
We created a new graphite-Cu(II) electrode and found that the electrode could catalyze FADH$_2$ oxidation and FAD reduction coupled to electricity production and consumption, respectively. In a fuel cell with graphite-Cu(II) anode and graphite-Fe(III) cathode, the electricity was produced by coupling to the spontaneous oxidation of FADH$_2$ Fumarate and xylose were not produced from the enzymatic oxidation of succinate and xylitol without FAD, respectively, but produced with FAD. The production of fumarate and xylose in the reactor with FAD electrochemically regenerated was maximally 2- 5 times higher than that in the reactor with FAD. By using this new electrode with catalytic function, a bioelectrocatalysts can be engineered; namely, oxidoreductase (e.g., lactate dehydrogenase) and FAD can function for biotransformation without an electron mediator and second oxidoreductase for cofactors recycling.
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