• 제목/요약/키워드: Oxidoreductase

검색결과 203건 처리시간 0.02초

Activity of Human Dihydrolipoamide Dehydrogenase Is Largely Reduced by Mutation at Isoleucine-51 to Alanine

  • Kim, Hak-Jung
    • BMB Reports
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    • 제39권2호
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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.

알저네이트 및 카이틴 고정화 Zymomonas mobilis 에 의한 쏠비톨의 연속생산 (Continuous Production of Sorbitol with Permeabilized Zymomonas mobilis Immobilized in Alginate and Chitin)

  • 최도진;김원극전억한
    • KSBB Journal
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    • 제5권3호
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    • pp.223-227
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    • 1990
  • Ethanol을 주로 생산하는 균주인 Z. mobilis의 cell wall 투과성을 높인 후 고정화하여 sorbitol 생산에 이용 하였다. 그러나, toluene으로 투과성을 높은 cell은 oxidoreductase의 유출, 손실로 인하여 sorbitol conversion efficency가 급격히 저하되었다. 따라서, 이와같은 enzymcd의 유출을 방지 하기 위하여, 투과성을 향상시킨 cell을 0.25% glutaraldehyd로 처리한 후 alginate와 chitin에 고정화하여 회석율 $0.2h^{-1}$에서 연속배양을 한 결과 210시간동안 효소활성도의 저하는 거의 일어나지 않았다. 이와같은 연속배양에서 얻어진 sorbitol productivity는 3.5g / l-h로 측정 되었다.

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Regulation of fpr Gene Encoding NADPH : Ferredoxin Oxidoreductase by the soxRS Locus in Escherichia coli

  • Koh, Young-Sang;Choih, Jenny;Roe, Jung-Hye
    • Journal of Microbiology
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    • 제34권2호
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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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Electrochemical Regeneration of FAD by Catalytic Electrode Without Electron Mediator and Biochemical Reducing Power

  • JEON SUNG JIN;SHIN IN HO;SANG BYUNG IN;PARK DOO HYUN
    • Journal of Microbiology and Biotechnology
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    • 제15권2호
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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.