Bifunctional phosphoglucose/phosphomannose isomerase from the hyperthermophilic archaeon Pyrobaculum aerophilum

Hansen, Thomas; Urbanke, Claus; Schönheit, Peter

doi:10.1007/s00792-004-0411-6

Cited by 22 publications

(25 citation statements)

References 13 publications

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“…However, the preliminary results indicated that the catalytic efficiency was very low (∼ 0.01 mM − 1 s − 1 ) with a glucose-6-phosphate dehydrogenase coupled reaction. 27 We therefore postulated that EcSI may be a sugar isomerase with alternative substrate specificity, which is also supported by the phenol bound in molecule B, as sugar-binding enzymes are often found to bind phenol as a substrate analogue, for example, UDP-galactose 4-epimerase, which binds UDP-phenol. 28 …”

Section: Ecsi Is Structurally Similar To Cupin Phosphoglucose Isomerasesmentioning

confidence: 99%

Structure-Based Annotation of a Novel Sugar Isomerase from the Pathogenic E. coli O157:H7

Staalduinen¹,

Park²,

Yeom³

et al. 2010

Journal of Molecular Biology

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Section: Ecsi Is Structurally Similar To Cupin Phosphoglucose Isomerasesmentioning

confidence: 99%

Structure-Based Annotation of a Novel Sugar Isomerase from the Pathogenic E. coli O157:H7

Staalduinen¹,

Park²,

Yeom³

et al. 2010

Journal of Molecular Biology

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“…acidophilum (see below). The coding sequences show low but detectable sequence similarities to the classical PGIs, especially in those residues involved in catalysis (82)(83)(84). However, in contrast to the G6P/F6P-specific conventional PGIs, the corresponding enzymes show promiscuous PGI and phosphomannose isomerase (PMI) activities, converting both G6P and mannose 6-phosphate (M6P) to F6P.…”

Section: Phosphoglucose Isomerasementioning

confidence: 99%

“…On the one hand, the similar core fold of PGI compared to that of PGI/PMI, the reaction mechanism, and the concomitant sequence conservation in functionally important residues clearly group the archaeal PGI/PMIs together with conventional PGIs into the same protein superfamily. On the other hand, the low overall sequence similarity accompanied by structural and mechanistic alterations facilitating the broader sub- strate spectrum define the conventional PGIs and the PGI/PMI enzymes as discrete protein families within the same superfamily (82,83,86).…”

Section: Figmentioning

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

273

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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“…The following controls were used. For His-tagged cPGIs, to correct for unspecific metal binding by the respective His tags as well as for H 2 O impurities, His-tagged glucose-6-phosphate dehydrogenase from T. maritima (23) and His-tagged PGI from P. aerophilum (25) were dialyzed and prepared as described above for the cPGIs, and the respective metal contents of the proteins were measured. The controls contained on average 0.02 Ni 2ϩ per enzyme molecule, whereas no iron could be detected in any of the control samples.…”

Section: Overexpression and Purification Of Recombinant Proteinmentioning

confidence: 99%

Cupin-Type Phosphoglucose Isomerases (Cupin-PGIs) Constitute a Novel Metal-Dependent PGI Family Representing a Convergent Line of PGI Evolution

et al. 2005

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Cupin-type phosphoglucose isomerases (cPGIs) were identified in some archaeal and bacterial genomes and the respective coding function of cpgi's from the euryarchaeota Archaeoglobus fulgidus and Methanosarcina mazei, as well as the bacteria Salmonella enterica serovar Typhimurium and Ensifer meliloti, was proven by functional overexpression. These cPGIs and the cPGIs from Pyrococcus and Thermococcus spp. represent the cPGI family and were compared with respect to kinetic, inhibitory, thermophilic, and metal-binding properties. cPGIs showed a high specificity for the substrates fructose-6-phosphate and glucose-6-phosphate and were inhibited by millimolar concentrations of sorbitol-6-phosphate, erythrose-4-phosphate, and 6-phosphogluconate. Treatment of cPGIs with EDTA resulted in a complete loss of catalytic activity, which could be regained by the addition of some divalent cations, most effectively by Fe 2؉ and Ni 2؉ , indicating a metal dependence of cPGI activity. The motifs TX 3 PX 3 GXEX 3 TXGHXHX 6-11 EXY and PPX 3 HX 3 N were deduced as the two signature patterns of the novel cPGI family. Phylogenetic analysis suggests lateral gene transfer for the bacterial cPGIs from euryarchaeota.Phosphoglucose isomerase (PGI; EC 5.3.1.9) catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. PGI plays a central role in sugar metabolism of eukarya, bacteria, and archaea, both in glycolysis via the Embden-Meyerhof pathway in eukarya and bacteria and in its modified versions found in archaea. PGI is also involved in gluconeogenesis, where the enzyme operates in the reverse direction (see references 22, 26, and 40). PGIs have evolved convergently. Most PGIs belong to the PGI superfamily, which can be divided into the PGI family and the recently identified bifunctional phosphoglucose/phosphomannose isomerase (PGI/PMI) family (22). PGIs from the PGI superfamily, often referred to as conventional PGIs, are found in all domains of life and are well studied. Crystal structures have been determined for the eukaryotic PGIs from pigs, rabbits, humans and from the bacterium Bacillus stearothermophilus, and conserved amino acids proposed to be involved in substrate binding and/ or catalysis have been identified (3, 6, 10-13, 28, 29, 42). Bifunctional PGI/PMIs, which have been characterized as a novel family within the PGI superfamily, were predominantly found in the crenarchaeotal branch of the archaea (26).Recently, a novel type of PGI has been identified and characterized from the hyperthermophilic euryarchaeon Pyrococcus furiosus (22, 52) and later from the closely related Thermococcus litoralis (30). These PGIs belong to the cupin superfamily and thus represent a convergent line of PGI evolution. The cupin superfamily is present in all three domains of life-eukarya, bacteria, and archaea-and comprises a group of functionally diverse proteins that contain a central domain composed of ␤-strands forming a small ␤-barrel called "cupin."Proteins from the cupin superfamily range, for example, from manno...

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Bifunctional phosphoglucose/phosphomannose isomerase from the hyperthermophilic archaeon Pyrobaculum aerophilum

Cited by 22 publications

References 13 publications

Structure-Based Annotation of a Novel Sugar Isomerase from the Pathogenic E. coli O157:H7

Structure-Based Annotation of a Novel Sugar Isomerase from the Pathogenic E. coli O157:H7

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

Cupin-Type Phosphoglucose Isomerases (Cupin-PGIs) Constitute a Novel Metal-Dependent PGI Family Representing a Convergent Line of PGI Evolution

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