The Hyperthermophilic Glycolytic Enzyme Enolase in the Archaeon, Pyrococcus furiousus: Comparison with Mesophilic Enolases

Peak, Meyrick J.; Peak, Jennifer G.; Stevens, Fred J.; Blamey, Jenny M.; Mai, Xuhong; Zhou, Zhao-Nian; Adams, Michael W. W.

doi:10.1006/abbi.1994.1389

Cited by 38 publications

(29 citation statements)

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“…Pyr. furiosus ENO depends on Mg 2ϩ ions for activity, which is common to all ENOs described so far (226). ENOs are abundant and highly conserved among all three domains of life (43,230).…”

Section: Enolasementioning

confidence: 96%

“…The conversion of 3PG to PEP proceeds via 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), which shows only remote similarity to its bacterial and eukaryotic counterparts (11% amino acid identity to the E. coli enzyme) (212), and enolase, which has been purified and characterized for Pyr. furiosus (226).…”

Section: Thermococcales (Pyrococcus Furiosus and Thermococcus Kodakarmentioning

confidence: 99%

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Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

Bräsen

Esser

Rauch

et al. 2014

Microbiol Mol Biol Rev

279

294

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SUMMARY The metabolism of Archaea , the third domain of life, resembles in its complexity those of Bacteria and lower Eukarya . However, this metabolic complexity in Archaea is accompanied by the absence of many “classical” pathways, particularly in central carbohydrate metabolism. Instead, Archaea are characterized by the presence of unique, modified variants of classical pathways such as the Embden-Meyerhof-Parnas (EMP) pathway and the Entner-Doudoroff (ED) pathway. The pentose phosphate pathway is only partly present (if at all), and pentose degradation also significantly differs from that known for bacterial model organisms. These modifications are accompanied by the invention of “new,” unusual enzymes which cause fundamental consequences for the underlying regulatory principles, and classical allosteric regulation sites well established in Bacteria and Eukarya are lost. The aim of this review is to present the current understanding of central carbohydrate metabolic pathways and their regulation in Archaea . In order to give an overview of their complexity, pathway modifications are discussed with respect to unusual archaeal biocatalysts, their structural and mechanistic characteristics, and their regulatory properties in comparison to their classic counterparts from Bacteria and Eukarya . Furthermore, an overview focusing on hexose metabolic, i.e., glycolytic as well as gluconeogenic, pathways identified in archaeal model organisms is given. Their energy gain is discussed, and new insights into different levels of regulation that have been observed so far, including the transcript and protein levels (e.g., gene regulation, known transcription regulators, and posttranslational modification via reversible protein phosphorylation), are presented.

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“…Pyr. furiosus ENO depends on Mg 2ϩ ions for activity, which is common to all ENOs described so far (226). ENOs are abundant and highly conserved among all three domains of life (43,230).…”

Section: Enolasementioning

confidence: 96%

Section: Thermococcales (Pyrococcus Furiosus and Thermococcus Kodakarmentioning

confidence: 99%

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

Bräsen

Esser

Rauch

et al. 2014

Microbiol Mol Biol Rev

279

294

View full text Add to dashboard Cite

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“…The oldest fossils include bacteria and other microorganisms that date to about 3.8 billion years ago (BYA). Glycolytic enzymes are evident in the Archean period, 2·BY before the earliest oxygenrequiring species and almost 4·BY before the present pathways (Gebbia et al, 1997;Kelly and Adams, 1994;Peak et al, 1994). Qualitative trends in the amount of global biomass are projected in Fig.·3B.…”

Section: Precambrian: Bacterial Glycolytic Genesmentioning

confidence: 99%

“…These are some of the most ancient and highly conserved proteins and genes known, with strong conservation of both the peptide and DNA sequences even between higher mammals and bacteria (Lonberg and Gilbert, 1985;Peak et al, 1994;Poorman et al, 1984). Fig.·2 shows a Southern blot illustrating the remarkable conservation of pyruvate kinase (PK) and lactate dehydrogenase (LDH) with strong crosshomology of DNA fragments between yeast and human DNA.…”

Section: Conservation Of Glycolytic Enzyme Genesmentioning

confidence: 99%

Evolution of the coordinate regulation of glycolytic enzyme genes by hypoxia

Webster

2003

Journal of Experimental Biology

149

107

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SUMMARYTwo billion years of aerobic evolution have resulted in mammalian cells and tissues that are extremely oxygen-dependent. Exposure to oxygen tensions outside the relatively narrow physiological range results in cellular stress and toxicity. Consequently, hypoxia features prominently in many human diseases, particularly those associated with blood and vascular disorders,including all forms of anemia and ischemia. Bioenergetic enzymes have evolved both acute and chronic oxygen sensing mechanisms to buffer changes of oxygen tension; at normal PO oxidative phosphorylation is the principal energy supply for eukaryotic cells, but when the PO falls below a critical mark metabolic switches turn off mitochondrial electron transport and activate anaerobic glycolysis. Without this switch cells would suffer an immediate energy deficit and death at low PO. An intriguing feature of the switching is that the same conditions that regulate energy metabolism also regulate bioenergetic genes, so that enzyme activity and transcription are regulated simultaneously,albeit with different time courses and signaling pathways. In this review we explore the pathways mediating hypoxia-regulated glycolytic enzyme gene expression, focusing on their atavistic traits and evolution.

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“…Numbers at the nodes are bootstrapping values according to neighbor joining (generated by using the NJ options of ClustalX). Enolases from Picrophilus torridus (PTO1234), Haloferax volcanii (HVO_2774), Thermoproteus tenax (GenBank accession number AJ621325), Sulfolobus solfataricus (GenBank accession number Q97ZJ3), E. coli (GenBank accession number P0A6P9), Bacillus subtilis (GenBank accession number P37869), Pyrococcus furiosus (PF0215) (56), and human (GenBank accession number P06733); fuconate dehydratases from Xanthomonas campestris (GenBank accession number Q8P3K2), human (GenBank accession number Q7L5Y1), and Xenopus laevis (GenBank accession number Q6INX4); rhamnonate dehydratases from Azotobacter vinelandii (PDB accession number 2OZ3), E. coli (PDB accession number 2I5Q), Sulfobacillus thermosulfidooxidans (GenBank accession number WP_053958247), and Scheffersomyces stipitis (GenBank accession number ABN68404); mannonate dehydratases (ManD-RspA) from Novosphingobium aromaticivorans (UniProt accession number A4XF23), E. coli (GenBank accession number P38104), and Streptomyces coelicolor (GenBank accession number P95726); promiscuous gluconate/ galactonate dehydratases (GAD/GalAD) from Thermoplasma acidophilum (Ta0085m), P. torridus (GenBank accession number Q6L1T2), S. solfataricus (GenBank accession number Q97U27), and S. acidocaldarius (Saci_0885); GAD from T. tenax (GenBank accession number CCC81796); and GAD and xylonate dehydratases (XAD) from H. volcanii (HVO_1488) (A), H. lacusprofundi (Hlac_1300), Haloarcula marismortui (rrnAC0575), H. volcanii (HVO_B0038A) (UniProt accession number D4GP40) (B), and Halorubrum lacusprofundi (Hlac_2242) are shown. sion of HVO_1488, purified recombinant GAD showed kinetic features similar to those of the native enzyme.…”

Section: Fig 5 Growth Analysis Of the H Volcanii Gad Deletion Mutantmentioning

confidence: 99%

Key Enzymes of the Semiphosphorylative Entner-Doudoroff Pathway in the Haloarchaeon Haloferax volcanii: Characterization of Glucose Dehydrogenase, Gluconate Dehydratase, and 2-Keto-3-Deoxy-6-Phosphogluconate Aldolase

et al. 2016

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The halophilic archaeon Haloferax volcanii has been proposed to degrade glucose via the semiphosphorylative Entner-Doudoroff (spED) pathway. So far, the key enzymes of this pathway, glucose dehydrogenase (GDH), gluconate dehydratase (GAD), and 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase (KDPGA), have not been characterized, and their functional involvement in glucose degradation has not been demonstrated. Here we report that the genes HVO_1083 and HVO_0950 encode GDH and KDPGA, respectively. The recombinant enzymes show high specificity for glucose and KDPG and did not convert the corresponding C 4 epimers galactose and 2-keto-3-deoxy-6-phosphogalactonate at significant rates. Growth studies of knockout mutants indicate the functional involvement of both GDH and KDPGA in glucose degradation. GAD was purified from H. volcanii, and the encoding gene, gad, was identified as HVO_1488. GAD catalyzed the specific dehydration of gluconate and did not utilize galactonate at significant rates. A knockout mutant of GAD lost the ability to grow on glucose, indicating the essential involvement of GAD in glucose degradation. However, following a prolonged incubation period, growth of the ⌬gad mutant on glucose was recovered. Evidence is presented that under these conditions, GAD was functionally replaced by xylonate dehydratase (XAD), which uses both xylonate and gluconate as substrates. Together, the characterization of key enzymes and analyses of the respective knockout mutants present conclusive evidence for the in vivo operation of the spED pathway for glucose degradation in H. volcanii. IMPORTANCEThe work presented here describes the identification and characterization of the key enzymes glucose dehydrogenase, gluconate dehydratase, and 2-keto-3-deoxy-6-phosphogluconate aldolase and their encoding genes of the proposed semiphosphorylative Entner-Doudoroff pathway in the haloarchaeon Haloferax volcanii. The functional involvement of the three enzymes was proven by analyses of the corresponding knockout mutants. These results provide evidence for the in vivo operation of the semiphosphorylative Entner-Doudoroff pathway in haloarchaea and thus expand our understanding of the unusual sugar degradation pathways in the domain Archaea. Glucose degradation in thermoacidophilic and halophilic archaea has been proposed to proceed via modified versions of the classical Entner-Doudoroff (ED) pathway of bacteria (1, 2) (Fig. 1). For the thermoacidophilic euryarchaeon Picrophilus torridus, a nonphosphorylative ED (npED) pathway was reported (3). Accordingly, glucose is converted to 2-keto-3-deoxygluconate (KDG) via glucose dehydrogenase (GDH) and gluconate dehydratase (GAD). KDG is then cleaved by a KDG aldolase to pyruvate and glyceraldehyde (GA), which is converted to a second molecule of pyruvate via glyceraldehyde dehydrogenase, 2-phosphoglycerate forming glycerate kinase, enolase, and pyruvate kinase. The pathway was proposed to be promiscuous, being involved in the degradation of both D-glucose and its C 4 epimer ...

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The Hyperthermophilic Glycolytic Enzyme Enolase in the Archaeon, Pyrococcus furiousus: Comparison with Mesophilic Enolases

Cited by 38 publications

References 0 publications

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

Evolution of the coordinate regulation of glycolytic enzyme genes by hypoxia

Key Enzymes of the Semiphosphorylative Entner-Doudoroff Pathway in the Haloarchaeon Haloferax volcanii: Characterization of Glucose Dehydrogenase, Gluconate Dehydratase, and 2-Keto-3-Deoxy-6-Phosphogluconate Aldolase

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