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

Mukund, Swarnalatha; Adams, Michael W. W.

doi:10.1016/s0021-9258(18)98669-2

Cited by 245 publications

(70 citation statements)

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“…Therefore, it was added to sta rt the reaction in a ll assays ofGAPOR, a nd activities were calcul ated from the first 10 s o f b e nzyl viologen reduction. The activities of AOR (9) and FOR (11) were dete rmined at 80 °C by the oxidation of crotonaldehyde a nd form aldehyde, respectively. GAPDH a ctivi ty was measured a t 70 °C by following the reduction of NAD at 340 nm (16).…”

Section: Methodsmentioning

confidence: 99%

“…10 and 11) have been purified. AOR oxidizes a range of aliphatic and aromatic aldehydes in vitro (9), whereas FOR utilizes only C1-C3 aldehydes. FOR is thought to function in peptide catabolism (11), whereas it was hypothesized that AOR catalyzed glyceraldehyde oxidation (9) as part of an unusual nonphosphorylated Entner-Doudoroff (ED) pathway.…”

mentioning

confidence: 99%

“…AOR oxidizes a range of aliphatic and aromatic aldehydes in vitro (9), whereas FOR utilizes only C1-C3 aldehydes. FOR is thought to function in peptide catabolism (11), whereas it was hypothesized that AOR catalyzed glyceraldehyde oxidation (9) as part of an unusual nonphosphorylated Entner-Doudoroff (ED) pathway. Most of the other enzymes of this ED pathway were subsequently demonstrated in cell extracts, albeit with very low activities (12).…”

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confidence: 99%

“…A similar study by others (14) also concluded that an EM type of pathway was present in P. furiosus, although a version of the ED pathway was also proposed. It is not clear, however, how an EM-type pathway could function in this organism, because cell extracts contain very low activities of two key glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase (PGK) (9,12,13,15). In fact, these enzymes are thought to function in gluconeogenesis when P. furiosus is grown on pyruvate (15).…”

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confidence: 99%

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Glyceraldehyde-3-phosphate Ferredoxin Oxidoreductase, a Novel Tungsten-containing Enzyme with a Potential Glycolytic Role in the Hyperthermophilic Archaeon Pyrococcus furiosus

Mukund

Adams

1995

Journal of Biological Chemistry

204

225

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The archaeon Pyrococcus furiosus grows optimally at 100 degrees C by the fermentation of carbohydrates to yield acetate, CO2, and H2. Cell-free extracts contain very low activity of the glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase, but extremely high activity of glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR). GAPOR was purified under strictly anaerobic conditions. It is a monomeric, O2-sensitive protein of M(r) approximately 63,000 which contains pterin and approximately 1 tungsten and 6 iron atoms per molecule. The enzyme oxidized glyceraldehyde-3-phosphate (Km 28 microM) to 3-phosphoglycerate and reduced P. furiosus ferredoxin (Km 6 microM), but it did not oxidize formaldehyde, acetaldehyde, glyceraldehyde, benzaldehyde, glucose, glucose 6-phosphate, or glyoxylate, nor did it use NAD(P) as an electron acceptor. It is proposed that GAPOR has a glycolytic role and functions in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Glyceraldehyde-3-phosphate Ferredoxin Oxidoreductase, a Novel Tungsten-containing Enzyme with a Potential Glycolytic Role in the Hyperthermophilic Archaeon Pyrococcus furiosus

Mukund

Adams

1995

Journal of Biological Chemistry

204

225

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“…This is further proved in our analysis, that the coding regions of enzymes or proteins involved in the above said metabolic processes are found to be homologues to the the noncoding regions of Aeropyrum pernix. Aldehyde ferredoxin oxido reductase is noted to play primary role in the catabolism of sugars or amino acids in Pyrococcus furiosus [12] and Thermococcus litoralis [13]. It is interesting to note that two different non coding regions upstream of APE_0167 and APE_0168.1 that are seen very close to each other show homology with coding region of the same enzyme aldehyde ferrodoxin oxido reductase which reveals that the activity of this enzyme is crucial in Aeropyrum pernix.…”

Section: Discussionmentioning

confidence: 94%

Insilico Identification of Novel Coding Regions From Archeal Genome - Aeropyrum Pernix

Arunmeena¹,

Shanmughavel²

2010

Int J of Bioi Res

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Researches on archaeal microorganisms continue to excite the scientific community. Their unique adaptations that cater to hypersaline, hyperthermic, and hypothermic circumstances have incited research to manipulate those attributes for use in virtually every aspect of life. Adaptations in membrane, enzymes, and protein structures and components have potential applications in areas including electronics, agriculture, aquaculture, medicine, pharmaceuticals, food science, and nutrition. Although the time and effort required to new find archaeal homologues may be great, many believe that the economic and environmental benefits of such a breakthrough would be considerable enough to outweigh the challenges. An analysis of the archeal genome Aeropyrum pernix, showed that certain regions earlier thought to be 'non-coding' have significant sequence similarity to other protein sequences from archaea and other species. The available sequence analysis tools were used to identify a number of potential protein coding regions in these putative 'non coding' regions. We could identify 907 such regions and 282 of them apparently code for proteins present in archeal or other species. The remaining 625 regions are mostly start /stop conflicts. Of the 282 protein coding regions, only 64 code for proteins with homologues of known function. A good number of proteins show homology to proteins that are important for the survival of the organism. Hence these novel regions may be referred as homologues to coding regions. In addition Genome sequence collections should be regularly checked to improve gene prediction by sequence similarity and greater effort is required to make gene definitions consistent across related species.

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Aldehyde Ferredoxin Oxidoreductase

Roy

Dhawan

Johnson

et al. 2004

Handbook of Metalloproteins

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Aldehyde ferredoxin oxidoreductase (AOR) is a homodimer where each subunit contains a [4Fe–4S] cluster and a mononuclear tungsten atom coordinated by the dithioline groups of two pterin molecules. The two subunits of the dimer are bridged by a monomeric iron site. AOR is a member of a family of five closely related tungstoenzymes found in organisms that grow at high temperatures in marine volcanic vents. The enzyme catalyzes the two‐electron oxidation of its aldehyde substrate to the corresponding acid with the concomitant reduction of ferredoxin, its physiological electron acceptor. The enzyme can oxidize a wide range of aliphatic and aromatic aldehydes. The most efficient substrates for AOR are acetaldehyde, isovaleraldehyde, phenylacetaldehyde, and indoleacetaldehyde, the aldehyde derivatives of some of the most common amino acids.

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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 245 publications

References 45 publications

Glyceraldehyde-3-phosphate Ferredoxin Oxidoreductase, a Novel Tungsten-containing Enzyme with a Potential Glycolytic Role in the Hyperthermophilic Archaeon Pyrococcus furiosus

Glyceraldehyde-3-phosphate Ferredoxin Oxidoreductase, a Novel Tungsten-containing Enzyme with a Potential Glycolytic Role in the Hyperthermophilic Archaeon Pyrococcus furiosus

Insilico Identification of Novel Coding Regions From Archeal Genome - Aeropyrum Pernix

Aldehyde Ferredoxin Oxidoreductase

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