The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase: Evidence for its participation in a unique glycolytic pathway.

Makund, S.; Adams, M.W.W.

doi:10.1016/0162-0134(91)84247-7

Cited by 83 publications

(184 citation statements)

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“…This has been shown for formate dehydrogenase from Clostridium formicoaceticum (Leonhardt and Andreesen, 1977), Clostridium thermoaceticum (Yamamoto et al, 1983), and Methanococcus vannielii (Jones and Stadtman, 1981), for carboxylic acid reductase from C. thermoaceticum (White et al, 1989) and C. formicoaceticum (White et al, 1991), for aldehyde: ferredoxin oxidoreductase and forma1dehyde:ferredoxin oxidoreductase from Pyrococcus furiosus and from Thermococcus litoralis Adams, 1991 and1993) and for some of the formylmethanofuran dehydrogenases (Schmitz et al, 1992a;Bertram et al, 1994). In addition to tungsten these enzymes contain a pterin cofactor (Schmitz et al, 1992a;Bertram et al, 1994;Johnson et al, 1993), indicating that the tungsten in these enzymes is coordinated similarly to molybdenum in the respective molybdenum enzymes (Cramer et al, 1985;George et al, 1992).…”

Section: Discussionmentioning

confidence: 83%

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

Bertram

Karrasch

Schmitz

et al. 1994

European Journal of Biochemistry

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Formylmethanofuran dehydrogenases, which are found in methanogenic Archaea, are molybdenum or tungsten iron-sulfur proteins containing a pterin cofactor. We report here on differences in substrate specificity, EPR properties and susceptibility towards cyanide inactivation of the enzymes from Methanosarcina barkeri, Methanobacterium thermoautotrophicum and Methanobacterium woljei.The molybdenum enzyme from M. barkeri (relative activity with N-formylmethanofuran = 100%) was found to catalyze, albeit at considerably reduced apparent V,,,,,, the dehydrogenation of N-furfurylformamide (11 %), N-methylformamide (0.2%), formamide (0.1 %) and formate (1 %). The molybdenum enzyme from M. wolfei could only use N-furfurylformamide (1 %) and formate (3 %) as pseudosubstrates. The molybdenum enzyme from M. thermoautotrophicum and the tungsten enzymes from M. thermoautotrophicum and M. wolfei were specific for N-formylmethanofuran.The molybdenum formylmethanofuran dehydrogenases exhibited at 77 K two rhombic EPR signals, designated FMDred and FMD,,, both derived from Mo as shown by isotopic substitution with 9 7 M~. The FMD,, signal was only displayed by the active enzyme in the reduced form and was lost upon enzyme oxidation; the FMD,, signal was displayed by an inactive form and was not quenched by 0,. The tungsten isoenzymes were EPR silent.The molybdenum formylmethanofuran dehydrogenases were found to be inactivated by cyanide whereas the tungsten isoenzymes, under the same conditions, were not inactivated. Inactivation was associated with a characteristic change in the molybdenum-derived EPR signal. Reactivation was possible in the presence of sulfide. Abbreviations. FMD,,,, EPR signal attributed to active formylmethanofuran dehydrogenase ; FMD,,, EPR signal attributed to inactive formylmethanofuran dehydrogenase ; R, Land6 splittina + co2 t P IE" = -497 mV (Thauer, 1990) factor; gx, gy-and g,, Land6 splitting factors in the x , y and directions for anisotropic systems; 1 U = 1 Fmol formylmethanofuran dehydrogenatedmin.The physiological electron accePtor/donor is not knownMethylviologen (E"' = -446 mV) can be used as artificial

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Section: Discussionmentioning

confidence: 83%

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

Bertram

Karrasch

Schmitz

et al. 1994

European Journal of Biochemistry

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“…In the npED branch, the bifunctional 2-keto-3-deoxy-(6-phospho)-gluconate (KD(P)G) aldolase, which is a key player in both branches, cleaves KDG into pyruvate and glyceraldehyde (Buchanan et al 1999;Lamble et al 2003;Lamble et al 2005;Ahmed et al 2005). Glyceraldehyde is then oxidized to glycerate by glyceraldehyde dehydrogenase Jung and Lee 2006) or glyceraldehyde oxidoreductase (Kardinahl et al 1999;Mukund and Adams 1991;Schicho et al 1993;Selig and Schönheit 1994). The subsequent phosphorylation by glycerate kinase (MOFRL family) results in the formation of 2-phosphoglycerate (Kehrer et al 2007;.…”

Section: Introductionmentioning

confidence: 99%

The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) of Sulfolobus solfataricus: a key-enzyme of the semi-phosphorylative branch of the Entner–Doudoroff pathway

et al. 2007

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Archaea utilize a branched modification of the classical Entner-Doudoroff (ED) pathway for sugar degradation. The semi-phosphorylative branch merges at the level of glyceraldehyde 3-phosphate (GAP) with the lower common shunt of the Emden-Meyerhof-Parnas pathway. In Sulfolobus solfataricus two different GAP converting enzymes-classical phosphorylating GAP dehydrogenase (GAPDH) and the non-phosphorylating GAPDH (GAPN)-were identified. In Sulfolobales the GAPN encoding gene is found adjacent to the ED gene cluster suggesting a function in the regulation of the semi-phosphorylative ED branch. The biochemical characterization of the recombinant GAPN of S. solfataricus revealed that-like the well-characterized GAPN from Thermoproteus tenax-the enzyme of S. solfataricus exhibits allosteric properties. However, both enzymes show some unexpected differences in co-substrate specificity as well as regulatory fine-tuning, which seem to reflect an adaptation to the different lifestyles of both organisms. Phylogenetic analyses and database searches in Archaea indicated a preferred distribution of GAPN (and/or GAP oxidoreductase) in hyperthermophilic Archaea supporting the previously suggested role of GAPN in metabolic thermoadaptation. This work suggests an important role of GAPN in the regulation of carbon degradation via modifications of the EMP and the branched ED pathway in hyperthermophilic Archaea.Keywords Glyceraldehyde-3-phosphate Á Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase Á GAPN Á Aldehyde dehydrogenase superfamily Á Branched Entner-Doudoroff pathway Á Carbohydrate metabolism Á Archaea Abbreviations EDEntner-Doudoroff sp Semi-phosphorylative np Non-phosphorylative EMP Embden-Meyerhof-Parnas G1P

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“…Absorption of both NADH and NADPH was measured at 340 nm (e = 6.22 M −1 ·cm −1 ), and NAD(P)H oxidation activities are given in micromoles per minute per milligram. Aldehyde ferredoxin oxidoreductase was measured by the oxidation of butyraldehyde (1 mM) with benzyl viologen (1 mM) as electron acceptor as described previously (35). V max and K m values of AdhA were calculated using nonlinear regression (nls function) in R (36).…”

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confidence: 99%

Single gene insertion drives bioalcohol production by a thermophilic archaeon

Basen

Schut

Nguyen

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Bioethanol production is achieved by only two metabolic pathways and only at moderate temperatures. Herein a fundamentally different synthetic pathway for bioalcohol production at 70°C was constructed by insertion of the gene for bacterial alcohol dehydrogenase (AdhA) into the archaeon Pyrococcus furiosus. The engineered strain converted glucose to ethanol via acetate and acetaldehyde, catalyzed by the host-encoded aldehyde ferredoxin oxidoreductase (AOR) and heterologously expressed AdhA, in an energy-conserving, redox-balanced pathway. Furthermore, the AOR/AdhA pathway also converted exogenously added aliphatic and aromatic carboxylic acids to the corresponding alcohol using glucose, pyruvate, and/or hydrogen as the source of reductant. By heterologous coexpression of a membrane-bound carbon monoxide dehydrogenase, CO was used as a reductant for converting carboxylic acids to alcohols. Redirecting the fermentative metabolism of P. furiosus through strategic insertion of foreign genes creates unprecedented opportunities for thermophilic bioalcohol production. Moreover, the AOR/AdhA pathway is a potentially game-changing strategy for syngas fermentation, especially in combination with carbon chain elongation pathways.Archaea | metabolic engineering | hyperthermophile | carbon monoxide | aldehydes

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The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase: Evidence for its participation in a unique glycolytic pathway.

Cited by 83 publications

References 0 publications

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) of Sulfolobus solfataricus: a key-enzyme of the semi-phosphorylative branch of the Entner–Doudoroff pathway

Single gene insertion drives bioalcohol production by a thermophilic archaeon

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