Ferrous-activated Nicotinamide Adenine Dinucleotide-linked Dehydrogenase from a Mutant of
            <i>Escherichia coli</i>
            Capable of Growth on 1,2-Propanediol

Sridhara, Sampath; Wu, Tai Te; Chused, Thomas M.; Lin, E. C. C.

doi:10.1128/jb.98.1.87-95.1969

Cited by 89 publications

(44 citation statements)

References 26 publications

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“…In addition to the adhE enzyme, there are two other ADH activities in E. coli [see 67,68]. One is 229 due to the NAD linked propanediol dehydrogenase [31,69]. This enzyme interconverts lactaldehyde and propanediol as part of the fermentation pathway for the methylpentoses fucose and rhamnose.…”

Section: Alcoholmentioning

confidence: 99%

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The fermentation pathways of Escherichia coli

Clark¹

1989

FEMS Microbiology Reviews

352

240

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Under anaerobic conditions and in the absence of alternative electron acceptors Escherichia coli converts sugars to a mixture of products by fermentation. The major soluble products are acetate, ethanol, acetate and formate with smaller amounts of succinate. In addition the gaseous products hydrogen and carbon dioxide are produced in substantial amounts. The pathway generating fermentation products is branched and the flow down each branch is varied in response both to the pH of the culture medium and the nature of the fermentation substrate. In particular, the ratio of the various fermentation products is manipulated in order to balance the number of reducing equivalents generated during glycolytic breakdown of the substrate. The enzymes and corresponding genes involved in these fermentation pathways are described. The regulatory responses of these genes and enzymes are known but the details of the underlying regulatory mechanisms are still obscure.

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Section: Alcoholmentioning

confidence: 99%

“…This enzyme interconverts lactaldehyde and propanediol as part of the fermentation pathway for the methylpentoses fucose and rhamnose. However it shows substantial activity toward ethanol, ethylene glycol, and other similar alcohols [69]. The E. coli propanediol dehydrogenase is homologous to the Zymomonas ADH isoenzyme II [70,71].…”

Section: Alcoholmentioning

confidence: 99%

The fermentation pathways of Escherichia coli

Clark¹

1989

FEMS Microbiology Reviews

352

240

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“…An NAD-linked 1,2-propanediol oxidoreductase has been partially purified from mutants of Escherichia coli capable of growing on the diol (Sridhara et al. 1969al. )…”

Section: ) I Ssi M 1 L a T I O N O F 12 -P R O P A N E D I O Lmentioning

confidence: 99%

Microbial metabolism of 1,2‐propanediol studied by the Rumen Simulation Technique (Rusitec)

Czerkawski

Piatková

Breckenridge

1984

Journal of Applied Bacteriology

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A series of experiments with the Rumen Simulation Technique (Rusitec) showed that 1,2-propanediol was metabolized efficiently by rumen micro-organisms and that the main end-products of fermentation were propionic and 2-methylbutyric acids. Propionaldehyde and n-propanol were also formed as intermediate compounds. The effect of the diol on digestion of the basal diet appeared to be small with concentrate, or when the roughage was supplemented with additional nitrogen (urea). The decrease in the output of acetic and butyric acids was consistent with utilization of C2 units for synthesis of 2-methylbutyric acid. The fermentation of 1,2-propanediol resulted in little or no increase in the output of additional microbial matter. The distribution of radioactivity from [1-14C]1,2-propanediol confirmed that propionaldehyde and n-propanol were the primary products of metabolism of the diol and that the end-products were propionic and 2-methylbutyric acids, with very little labelling of microbial matter. Between 2% and 3% of radioactivity was found in gases and surprisingly the specific radioactivity of methane was higher than that of carbon dioxide, particularly during the initial stages of incubation. Possible pathways in the degradation of 1,2-propanediol by rumen micro-organisms are suggested and discussed in relation to similar reactions established in other systems.

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“…Indeed, the presence of iron has been clearly identified only in ADH II from Z. mobilis [27Ϫ29] and ADH E from E. coli [30], while other members of this family have been reported to bind metal ions other than iron [31Ϫ33]. In the case of POR, it was known that ferrous and manganous ions reactivate the enzyme, whereas zinc causes complete inactivation [26], although, at present no information on the enzymebound metal or the specific amino acid participation in the binding center has been reported.…”

Section: Discussionmentioning

confidence: 99%

“…Both V263C and C362I mutants presented a decrease in catalytic efficiency of threefold and tenfold, respectively. Wild-type POR is known to be inactivated by zinc [26]. A plot of the apparent first-order rate constants for inactivation (k obs ) at various concentrations of ZnCl 2 allows the calculation of the second-order rate constant of inactivation, which was 9090 M Ϫ1 min Ϫ1 for wild-type and 1900 M Ϫ1 min Ϫ1 and 555 M Ϫ1 min Ϫ1 for V262C and C363I mutants, respectively, implying a destabilized metal-binding site with lower affinity for zinc in the mutant enzymes.…”

Section: Kinetic Measurementsmentioning

confidence: 99%

Site‐directed mutagenesis studies of the metal‐binding center of the iron‐dependent propanediol oxidoreductase from Escherichia coli

Obradors

Cabiscol

Aguilar

et al. 1998

European Journal of Biochemistry

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The amino acid residues involved in the metal-binding site in the iron-containing dehydrogenase family were characterized by the site-directed mutagenesis of selected candidate residues of propanediol oxidoreductase from Escherichia coli. Based on the findings that mutations H263R, H267A and H277A resulted in iron-deficient propanediol oxidoreductases without catalytic activity, we identified three conserved His residues as iron ligands, which also bind zinc. The Cys362, a residue highly conserved among these dehydrogenases, was considered another possible ligand by comparison with the sequences of the medium-chain dehydrogenases. Mutation of Cys362 to Ile, resulted in an active enzyme that was still able to bind iron, with minor changes in the K m values and decreased thermal stability. Furthermore, in an attempt to produce an enzyme specific only for the zinc ion, three mutations were designed to mimic the catalytic zinc-binding site of the medium-chain dehydrogenases: (1) V262C produced an enzyme with altered kinetic parameters which nevertheless retained a significant ability to bind both metals, (2) the double mutant V262CϪM265D was inactive and too unstable to allow purification, and (3) the insertion of a cysteine at position 263 resulted in a catalytically inactive enzyme without iron-binding capacity, while retaining the ability to bind zinc. This mutation could represent a conceivable model of one of the steps in the evolution from iron to zinc-dependent dehydrogenases.

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Ferrous-activated Nicotinamide Adenine Dinucleotide-linked Dehydrogenase from a Mutant of Escherichia coli Capable of Growth on 1,2-Propanediol

Abstract: A nicotinamide adenine dinucleotide-linked dehydrogenase has been partially purified from a mutant of Escherichia coli K-12 able to grow on L-1 ,2-propanediol as carbon and energy source. This enzyme catalyzes the dehydrogenation at carbon

Cited by 89 publications

References 26 publications

The fermentation pathways of Escherichia coli

The fermentation pathways of Escherichia coli

Microbial metabolism of 1,2‐propanediol studied by the Rumen Simulation Technique (Rusitec)

Site‐directed mutagenesis studies of the metal‐binding center of the iron‐dependent propanediol oxidoreductase from Escherichia coli

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