A Class II fructose-1 ,6-bisphosphate aldolase from a halophilic archaebacterium Haloferax mediterranei.

D'Souza, Sandra E.; Altekar, Wijaya

doi:10.2323/jgam.44.235

Cited by 6 publications

(6 citation statements)

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“…Characterization of 1-PFK showed a 36-fold-higher catalytic efficiency of the enzyme for F1P than for F6P (k cat /K m values of 1.2 ϫ 10 6 s Ϫ1 M Ϫ1 for F1P and 0.034 ϫ 10 6 s Ϫ1 M Ϫ1 for F6P). For FBPA, bacterial-like class II activity with Mn 2ϩ as the preferred divalent cation was demonstrated (123,132). The phylogenetic distribution of bacterial-type class II FBPAs is restricted to a few haloarchaeal species, and acquisition via lateral gene transfer from Bacteria has been suggested (123).…”

Section: Fig 27mentioning

confidence: 99%

“…Although these archaeal-type class I enzymes have been reported for most Archaea, including many extreme halophiles, and therefore might represent the typical archaeal FBPA (126,137), for Haloferax species as well as some other haloarchaea, class II enzymes have been reported and characterized in detail (123,132). These halophilic class II aldolases represent the only archaeal class II aldolases known so far.…”

Section: Fructose-16-bisphosphate Aldolase (Catabolic)mentioning

confidence: 99%

“…In accordance with the E. coli enzyme, the halophilic class II aldolases are 100-kDa homodimers (50-kDa subunits), share the conserved residues involved in catalysis, and were described to prefer Fe 2ϩ or Mn 2ϩ instead of Zn 2ϩ as a bivalent metal ion. Phylogenetic analyses revealed that the haloarchaeal sequences form a distinct third subfamily within the class II FBPA family, and it has been speculated that haloarchaea acquired these enzymes from Bacteria in a horizontal gene transfer event (123,132). The archaeal class I aldolases have been proposed to represent early descendants of an ancient lineage separated very early from the lineages of classical class I and class II aldolases (126).…”

Section: Fructose-16-bisphosphate Aldolase (Catabolic)mentioning

confidence: 99%

“…furiosus, and Tco. kodakarensis (126,130,132,133). Two classes of FBPAs, which differ with respect to reaction mechanisms and distributions in the biosphere, have been identified (for literature, see reference 134).…”

Section: Fructose-16-bisphosphate Aldolase (Catabolic)mentioning

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

271

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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Section: Fig 27mentioning

confidence: 99%

Section: Fructose-16-bisphosphate Aldolase (Catabolic)mentioning

confidence: 99%

Section: Fructose-16-bisphosphate Aldolase (Catabolic)mentioning

confidence: 99%

Section: Fructose-16-bisphosphate Aldolase (Catabolic)mentioning

confidence: 99%

See 2 more Smart Citations

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

Bräsen

Esser

Rauch

et al. 2014

Microbiol Mol Biol Rev

271

294

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“…Although several enzymes of the proposed modified EM pathway in haloarchaea, ketohexokinase, 1-PFK, and class I and class II type FBA, have been purified (21,31,36,37), the genes encoding these enzymes have not been identified so far, and their functional involvement in fructose catabolism has not been demonstrated. Recently, the fructose-specific upregulation of a gene (HVO_1500) encoding putative 1-PFK has been reported for H. volcanii, and the role of a transcription regulator (GlpR) in fructose catabolism has been analyzed (39).…”

mentioning

confidence: 99%

Fructose Degradation in the Haloarchaeon Haloferax volcanii Involves a Bacterial Type Phosphoenolpyruvate-Dependent Phosphotransferase System, Fructose-1-Phosphate Kinase, and Class II Fructose-1,6-Bisphosphate Aldolase

2012

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The halophilic archaeon Haloferax volcanii utilizes fructose as a sole carbon and energy source. Genes and enzymes involved in fructose uptake and degradation were identified by transcriptional analyses, deletion mutant experiments, and enzyme characterization. During growth on fructose, the gene cluster HVO_1495 to HVO_1499, encoding homologs of the five bacterial phosphotransferase system (PTS) components enzyme IIB (EIIB), enzyme I (EI), histidine protein (HPr), EIIA, and EIIC, was highly upregulated as a cotranscript. The in-frame deletion of HVO_1499, designated ptfC (ptf stands for phosphotransferase system for fructose) and encoding the putative fructose-specific membrane component EIIC, resulted in a loss of growth on fructose, which could be recovered by complementation in trans. Transcripts of HVO_1500 (pfkB) and HVO_1494 (fba), encoding putative fructose-1-phosphate kinase (1-PFK) and fructose-1,6-bisphosphate aldolase (FBA), respectively, as well as 1-PFK and FBA activities were specifically upregulated in fructose-grown cells. pfkB and fba knockout mutants did not grow on fructose, whereas growth on glucose was not inhibited, indicating the functional involvement of both enzymes in fructose catabolism. Recombinant 1-PFK and FBA obtained after homologous overexpression were characterized as having kinetic properties indicative of functional 1-PFK and a class II type FBA. From these data, we conclude that fructose uptake in H. volcanii involves a fructose-specific PTS generating fructose-1-phosphate, which is further converted via fructose-1,6-bisphosphate to triose phosphates by 1-PFK and FBA. This is the first report of the functional involvement of a bacterial-like PTS and of class II FBA in the sugar metabolism of archaea. Various halophilic archaea, including Haloarcula marismortui and Haloferax volcanii, have been reported to utilize fructose as carbon and energy sources (29,34,46). The pathway of fructose degradation has been studied so far mainly in the Haloarcula species H. vallismortis and H. marismortui (6,7,29). On the basis of enzyme analyses, a modified version of the Embden-Meyerhof (EM) pathway has been proposed, involving fructose phosphorylation via ketohexokinase to fructose-1-phosphate, which is further phosphorylated to fructose-1,6-bisphosphate (FBP) by fructose-1-phosphate kinase (1-PFK). FBP is subsequently cleaved by FBP aldolase (FBA) to dihydroxyacetone phosphate and glyceraldehyde-3-phosphate, which are degraded to pyruvate following classical enzymes of the EM pathway. In vivo evidence for the operation of an EM pathway in fructose degradation was demonstrated in H. marismortui by labeling experiments with [13 C]fructose using growing cultures (29). With the same labeling techniques, glucose degradation in H. marismortui was shown to be degraded in vivo via an Entner-Doudoroff (ED) type pathway (29), which is in accordance with the proposed semiphosphorylated ED pathway for glucose degradation in haloarchaea (43).Although several enzymes of the proposed modified EM pathway...

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Properties of Halophilic Proteins

2003

Cellular Origin, Life in Extreme Habitats and Astrobiology

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A Class II fructose-1 ,6-bisphosphate aldolase from a halophilic archaebacterium Haloferax mediterranei.

Cited by 6 publications

References 42 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

Fructose Degradation in the Haloarchaeon Haloferax volcanii Involves a Bacterial Type Phosphoenolpyruvate-Dependent Phosphotransferase System, Fructose-1-Phosphate Kinase, and Class II Fructose-1,6-Bisphosphate Aldolase

Properties of Halophilic Proteins

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