Glycerate kinase of the hyperthermophilic archaeon Thermoproteus tenax: new insights into the phylogenetic distribution and physiological role of members of the three different glycerate kinase classes

Daniel, Kehrer; Ahmed, Hatim; Brinkmann, Henner; Siebers, Bettina

doi:10.1186/1471-2164-8-301

Cited by 23 publications

(39 citation statements)

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“…Although several enzymes of this pathway have been characterized, their regulatory properties have not been addressed. So far the glycerate kinase of T. tenax has been the only enzyme that was shown to exhibit regulatory properties (competitive inhibition via ADP) and regulation by the energy charge of the cell has been suggested (Kehrer et al 2007). During the re-evaluation of the modified ED pathway in Archaea, we encountered a partially conserved gene cluster composed of genes encoding gluconate dehydratase (gad) Kim and Lee 2005;Ahmed et al 2005), KDG kinase (kdgK) (Ahmed et al 2005;Lamble et al 2005) and KD(P)G aldolase (kdgA) (Ahmed et al 2005;Buchanan et al 1999;Lamble et al 2005;Theodossis et al 2004) (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…However, recent combinations of genomics-based and biochemical analyses demonstrated the presence of the branched ED pathway in all Archaea that utilize the ED pathway (Siebers et al 2004;Ahmed et al 2005;Jung and Lee 2005;Kehrer et al 2007). The only exception known so far is Halobacterium sp.…”

Section: Introductionmentioning

confidence: 99%

“…The only exception known so far is Halobacterium sp. NRC-1, which harbors no known glycerate kinase homolog and thus seems to rely on the spED pathway for glucose degradation (Kehrer et al 2007).…”

Section: Introductionmentioning

confidence: 99%

“…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;. Finally, pyruvate is formed by the combined action of enolase and pyruvate kinase (De Rosa et al 1984;Selig et al 1997).…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…Glycerate 2-kinases are involved in the degradation of Glc and other metabolic pathways in animals and bacteria (Guo et al, 2006;Kehrer et al, 2007) but have not been reported for plants. Instead, a glycerate 3-kinase (GLYK) occurs in plant chloroplasts and many cyanobacteria, where it produces glycerate 3-phosphate (3PGA) from glycerate in the last step of the photorespiratory C 2 cycle (Boldt et al, 2005;Bartsch et al, 2008).…”

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confidence: 99%

An Autoinhibitory Domain Confers Redox Regulation to Maize Glycerate Kinase

Bartsch

Mikkat²,

Hagemann

et al. 2010

Plant Physiology

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Glycerate 3-kinase (GLYK) is the terminal enzyme of the photorespiratory cycle in plants and many cyanobacteria. For several C 4 plants, notably grasses of the NADP-malic enzyme (ME) subtype, redox regulation of GLYK has been reported, but the responsible molecular mechanism is not known. We have analyzed the enzyme from the NADP-ME C 4 plant maize (Zea mays) and found that maize GLYK, in contrast to the enzyme from C 3 plants and a dicotyledonous NADP-ME C 4 plant, harbors a short carboxy-terminal extension. In its oxidized (night) form, a disulfide bridge is formed between the two cysteine residues present in this extra domain, and GLYK activity becomes inhibited. Cleavage of this bond by thioredoxin f produces the fully active thiol form, releasing autoinhibition. Fusion of the maize GLYK redox-regulatory domain to GLYK from C 3 plants confers redox regulation to these otherwise unregulated enzymes. It appears that redox regulation of GLYK could be an exclusive feature of monocotyledonous C 4 plants of the NADP-ME type, in which linear electron transport occurs only in the mesophyll chloroplasts. Hence, we suggest that GLYK, in addition to its function in photorespiration, provides glycerate 3-phosphate for the accelerated production of triose phosphate and its export from the mesophyll. This could facilitate the activation of redoxregulated Calvin cycle enzymes and the buildup of Calvin cycle intermediates in the bundle sheath of these particular C 4 plants during the dark/light transition.

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Biocatalytic Asymmetric Phosphorylation Catalyzed by Recombinant Glycerate‐2‐Kinase

Hardt¹,

Kinfu

Chow

et al. 2017

ChemBioChem

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The efficient synthesis of pure d-glycerate-2-phosphate is of great interest due to its importance as an enzyme substrate and metabolite. Therefore, we investigated a straightforward one-step biocatalytic phosphorylation of glyceric acid. Glycerate-2-kinase from Thermotoga maritima was expressed in Escherichia coli, allowing easy purification. The selective glycerate-2-kinase-catalyzed phosphorylation was followed by P NMR and showed excellent enantioselectivity towards phosphorylation of the d-enantiomer of glyceric acid. This straightforward phosphorylation reaction and subsequent product isolation enabled the preparation of enantiomerically pure d-glycerate 2-phosphate. This phosphorylation reaction, using recombinant glycerate-2-kinase, yielded d-glycerate 2-phosphate in fewer reaction steps and with higher purity than chemical routes.

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Glycerate kinase of the hyperthermophilic archaeon Thermoproteus tenax: new insights into the phylogenetic distribution and physiological role of members of the three different glycerate kinase classes

Cited by 23 publications

References 66 publications

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

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

An Autoinhibitory Domain Confers Redox Regulation to Maize Glycerate Kinase

Biocatalytic Asymmetric Phosphorylation Catalyzed by Recombinant Glycerate‐2‐Kinase

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