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  • 1
    Electronic Resource
    Electronic Resource
    Electron transport chain of Zymomonas mobilis (1990)
    Springer
    Archives of microbiology 154 (1990), S. 536-543 
    Details
    ISSN: 1432-072X
    Keywords: Zymomonas mobilis ; Glucose dehydrogenase ; Pyrroloquinoline quinone ; Ubiquinone ; Electron transport chain ; TMPD oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The interaction of the membrane-bound glucose dehydrogenase from the anaerobic but aerotolerant bacterium Zymomonas mobilis with components of the electron transport chain has been studied. Cytoplasmic membranes showed reduction of oxygen to water with the substrates glucose or NADH. The effects of the respiratory chain inhibitors piericidin, capsaicin, rotenone, antimycin, myxothiazol, HQNO, and stigmatellin on the oxygen comsumption rates in the presence of NADH or glucose as substrates indicated that a complete and in the most parts identical respiratory chain is participating in the glucose as well as in the NADH oxidation. Furthermore, the presence of coenzyme Q10 (ubiquinone 10) in Z. mobilis was demonstrated. Extraction from and reincorporation of the quinone into the membranes revealed that ubiquinone is essential for the respiratory activity with glucose and NADH. In addition, a membrane-associated tetramethyl-p-phenylene-diamine-oxidase activity could be detected in Z. mobilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248833
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  • 2
    Electronic Resource
    Electronic Resource
    Formation of acetyl-CoA in Zymomonas mobilis by a pyruvate dehydrogenase complex (1993)
    Springer
    Archives of microbiology 159 (1993), S. 197-199 
    Details
    ISSN: 1432-072X
    Keywords: Zymomonas mobilis ; Pyruvate dehydrogenase multienzyme complex ; Anaerobic formation of acetyl-CoA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the gram negative, obligately ethanologenic bacterium Zymomonas mobilis a pyruvate dehydrogenase complex was identified and the complex was enriched from cell extracts. This multienzyme complex is responsible for acetyl-CoA biosynthesis from pyruvate. No activities of related multienzyme complexes, 2-ketoglutarate dehydrogenase and branched chain keto acid dehydrogenase, could be detected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00250282
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation of the dxr gene of Zymomonas mobilis and characterization of the 1-deoxy-D-xylulose 5-phosphate reductoisomerase (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 191 (2000), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The gene encoding the second enzyme of the 2C-methyl-D-erythritol 4-phosphate (MEP) pathway for isopentenyl diphosphate biosynthesis, 1-deoxy-D-xylulose 5-phosphate (DXP) reductoisomerase, was cloned and sequenced from Zymomonas mobilis. The deduced amino acid sequence showed the highest identity (48.2%) to the DXP reductoisomerase of Escherichia coli. Biochemical characterization of the purified DXP reductoisomerase showed a strict dependence of the enzyme on NADPH and divalent cations (Mn2+, Co2+ or Mg2+). The enzyme is a dimer with a molecular mass of 39 kDa per subunit and has a specific activity of 19.5 U mg protein−1. Catalysis of the intramolecular rearrangement and reduction of DXP to MEP is competitively inhibited by the antibiotic fosmidomycin with a Ki of 0.6 μM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2000.tb09329.x
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  • 4
    Electronic Resource
    Electronic Resource
    Exceptional characteristics of heterotetrameric (α2β2) E1p of the pyruvate dehydrogenase complex from Zymomonas mobilis: expression from an own promoter and a lipoyl domain in E1β (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 177 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In the pyruvate dehydrogenase complex (PDHC) of Zymomonas mobilis the β subunit of the pyruvate dehydrogenase (E1p) as well as the acetyltransferase (E2p) contain an N-terminal lipoyl domain. Both lipoyl domains were acetylated in vitro using 2-14C-pyruvate as a substrate, demonstrating that both lipoyl domains can accept acetyl groups from the E1 component. As previously shown the structural genes (pdhAαβ, pdhB, lpd) encoding the pyruvate dehydrogenase complex of Z. mobilis are located in two distinct gene clusters, pdhAαβ and pdhB-orf2-lpd (U. Neveling et al. (1998) J. Bacteriol. 180, 1540–1548). Analysis of pdh gene expression using lacZ fusions revealed that the DNA fragments upstream of pdhAα, pdhB and lpd each have promoter activities. These pdh promoter activities were 7–30-fold higher in Z. mobilis than in Escherichia coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13721.x
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  • 5
    Electronic Resource
    Electronic Resource
    Influence of ethanol on the activities of 3-hydroxy-3-methylglutaryl-coenzyme A-reductase and squalene-hopene-cyclase in Zymomonas mobilis (1989)
    Springer
    Applied microbiology and biotechnology 30 (1989), S. 170-175 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The influence of different primary aliphatic alcohols on the activities of two key enzymes in hopanoid biosynthesis of Zymomonas mobilis was investigated. By use of 14C- and 3H-labelled substrates the enzymes 3-hydroxy-3-methylglutaryl-CoA-reductase and squalene-hopenecyclase were detected with activities of 1.6 pmol x (min x mg protein)-1 and 2.3 pmol x- (min x mg protein)-1, respectively. Cells grown in the presence of 6% (v/v) ethanol did not show higher activities of these enzymes than cells grown in the presence of 1% (v/v) ethanol. Furthermore, 3-hydroxy-3-methylglutaryl-CoA-reductase was not activated by ethanol. However, ethanol activated the squalene-hopene-cyclase when added to the enzyme test system. Besides ethanol, propanol also had a positive effect on the squalene-hopene-cyclase: the enzyme's activity increased 1.7-fold in the presence of either alcohol at a concentration of 6% (v/v). This corresponded with a similar increase of hopanoid content of whole cells when grown in the presence of 6% (v/v) added ethanol or propanol. These results indicated that the squalene-hopene-cyclase has a regulatory function in the alcohol dependent hopanoid biosynthesis of Z. mobilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264007
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  • 6
    Electronic Resource
    Electronic Resource
    Zymomonas mobilis mutants blocked in fructose utilization (1985)
    Springer
    Applied microbiology and biotechnology 23 (1985), S. 134-139 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A mutant ofZymomonas mobilis deficient in the utilization of fructose for growth and ethanol formation was shown to lack fructokinase activity. When grown in media which contained glucose+fructose or sucrose, both the mutant and wild type produced sorbitol in amounts up to 60 g·l-1, depending on the initial concentrations of sugars. Sorbitol formation was accompanied by an accumulation of acetaldehyde, gluconate, and acetoin. A ferricyanide-dependent sorbitol dehydrogenase could be localized in the cell membrane; it thus resembles the sorbitol dehydrogenase ofGluconobacter suboxydans. Neither a NAD(P)H dependent reduction of fructose nor a NAD(P) dependent dehydrogenation of sorbitol could be detected in cell-free extracts. The use of fructose-negative mutants ofZ. mobilis for the enrichment of fructose in glucose+fructose mixtures is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00938966
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  • 7
    Electronic Resource
    Electronic Resource
    Effect of alcohols and temperature on the hopanoid content of Zymomonas mobilis (1986)
    Springer
    Applied microbiology and biotechnology 25 (1986), S. 32-36 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The influence of different culture conditions on the hopanoid content of Zymomonas mobilis was investigated in batch cultures. With a gas-liquid chromatographic method it could be shown that the content of 1,2,3,4-tetrahydroxypentane-29-hopane (THBH) reached a maximum value in the stationary phase due to the high level of ethanol accumulated in the medium. The hopanoid content increased sharply with the addition of ethanol to the culture. Ethanol was shown to be the most effective of the alcohols tested in causing an increase of the hopanoid content. Furthermore, an alteration of the incubation temperature from 14° to 37°C also caused an increase of the amount of hopanoids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252509
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  • 8
    Electronic Resource
    Electronic Resource
    Formation and degradation of gluconate by Zymomonas mobilis (1988)
    Springer
    Applied microbiology and biotechnology 27 (1988), S. 378-382 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Zymomonas mobilis ATCC 29191 is able to degrade gluconate but cannot use it as a single carbon and energy source. Gluconate is phosphorylated by a gluconate kinase (EC 2.7.1.12) and the resulting 6-phosphogluconate is further catabolized to yield about 0.8 mol ethanol per mol of gluconate, considerable amounts of acetate and acetoin. This product spectrum agrees with the theoretical yield of only one reduction equivalent if gluconate is phosphorylated by a kinase and subsequently metabolized via the Entner-Doudoroff pathway. Furthermore, Z. mobilis contains a membrane-bound enzyme system which is able to oxidize glucose to gluconate. Cell-free extracts were active in an assay system with Wurster's blue as electron acceptor, and various aldoses as well as maltose, mannitol and sorbitol could be oxidized. The affinity for sorbitol was very low (K m =330 mM) but reasonable for glucose (K m =2.8 mM). The pH optimum for the glucose-oxidizing reaction was 6.5, while that for sorbitol oxidation was 5.5.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00251772
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  • 9
    Electronic Resource
    Electronic Resource
    Zymomonas mobilis mutants blocked in fructose utilization (1985)
    Springer
    Applied microbiology and biotechnology 23 (1985), S. 134-139 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A mutant ofZymomonas mobilis deficient in the utilization of fructose for growth and ethanol formation was shown to lack fructokinase activity. When grown in media which contained glucose+fructose or sucrose, both the mutant and wild type produced sorbitol in amounts up to 60 g·l-1, depending on the initial concentrations of sugars. Sorbitol formation was accompanied by an accumulation of acetaldehyde, gluconate, and acetoin. A ferricyanide-dependent sorbitol dehydrogenase could be localized in the cell membrane; it thus resembles the sorbitol dehydrogenase ofGluconobacter suboxydans. Neither a NAD(P)H dependent reduction of fructose nor a NAD(P) dependent dehydrogenation of sorbitol could be detected in cell-free extracts. The use of fructose-negative mutants ofZ. mobilis for the enrichment of fructose in glucose+fructose mixtures is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01982730
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  • 10
    Electronic Resource
    Electronic Resource
    Junctions of catabolic and anabolic pathways in Zymomonas mobilis: phosphoenolpyruvate carboxylase and malic enzyme (1989)
    Springer
    Applied microbiology and biotechnology 31 (1989), S. 529-536 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The synthesis of oxalacetate and malate in the ethanol-producing bacterium Zymomonas mobilis have been investigated. Cell-free extracts were examined for pyruvate carboxylase, phosphoenolpyruvate (PEP) carboxylase, PEP carboxytransphosphorylase, PEP carboxykinase, and malic enzyme, but only PEP carboxylase and nicotine adenine dinucleotide (NAD)-dependent malic enzyme activities could be detected. The PEP carboxylase, partially purified from extracts, was not affected by acetyl-coenzyme A. Intermediates of the tricarboxylic acid cycle and aspartate inhibited the enzyme competitively with PEP. Of these, citrate and α-ketoglutarate were the strongest inhibitors. The physiological roles of PEP carboxylase and malic enzyme in Z. mobilis are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00270789
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