Presence of a Novel Phosphopentomutase and a 2-Deoxyribose 5-Phosphate Aldolase Reveals a Metabolic Link between Pentoses and Central Carbon Metabolism in the Hyperthermophilic Archaeon
            <i>Thermococcus kodakaraensis</i>

Rashid, Naeem; Imanaka, Hiroyuki; Fukui, Toshiaki; Atomi, Haruyuki; Imanaka, Tadayuki

doi:10.1128/jb.186.13.4185-4191.2004

Cited by 50 publications

(49 citation statements)

References 31 publications

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“…From the presence of both enzyme activities in crude extracts of starch-and pyruvate-grown cells of Tco. kodakarensis, the physiological importance of this pathway was concluded, and a biosynthetic function was proposed (385). However, the pathway seems to be restricted to only a few archaeal species, and the physiological significance remains unclear.…”

Section: Alternative Pathways For C 5 -C 3 Interconversionmentioning

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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Section: Alternative Pathways For C 5 -C 3 Interconversionmentioning

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

View full text Add to dashboard Cite

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“…Interestingly, a structurally novel phosphopentomutase was characterized in Thermococcus kodakaraensis, which is similar to phosphomannomutases within COG1109 (Rashid et al, 2004). We searched for COG1109-related sequences in genome-sequenced mollicutes and analyzed the genomic position of each retrieved sequence.…”

Section: Purine and Pyrimidine Nucleotide Pathways In Mollicutesmentioning

confidence: 99%

Purine and pyrimidine nucleotide metabolism in Mollicutes

Bizarro

Schuck

2007

Genet. Mol. Biol.

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Several mollicute genome projects are underway, offering unique opportunities to study genes and metabolic pathways on a genome-wide scale. Here, we have analyzed the conservation and diversity of purine and pyrimidine metabolism in mycoplasmas. An evaluation of discrepancies between genomic analysis and enzymatic data revealed interesting aspects about these organisms. We found important examples in which enzyme activity was reported without the annotation of a corresponding gene. An interesting example concerns phosphopentomutase. In Mollicutes, we have identified CDSs orthologous to sequences recently identified as new phosphopentomutases in archaeobacteria that are structurally related to phosphomannomutases. It is suggested that these sequences could replace the function of phosphopentomutases in mollicutes lacking the canonical phosphopentomutase gene (deoB). Also, the activity of 5'-nucleotidase was reported in mollicutes that do not possess any CDS related to ushA. Hypothetical proteins exhibiting domains similar to newly characterized 5' nucleotidases in Escherichia coli are proposed as possible CDSs related to this enzymatic activity in Mollicutes. Based on our analysis, the reductive genome evolution of Mollicutes does not appear to result in a minimum set of genes nor a minimum set of metabolic functions shared by all mollicute species.

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“…Most bacterial phosphopentomutases characterized so far belong to the same protein family as alkaline phosphatases, sulfatases, and cofactor-independent bisphosphoglycerate mutases (1), though the enzyme from Thermococcus kodakaraensis belongs to the same protein family as mammalian phosphoglucomutase 1 (PGM1), 5 the enzyme that catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate (2).…”

mentioning

confidence: 99%

Molecular Identification of Mammalian Phosphopentomutase and Glucose-1,6-bisphosphate Synthase, Two Members of the α-D-Phosphohexomutase Family

Maliekal¹,

Соколова

Vertommen³

et al. 2007

Journal of Biological Chemistry

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The molecular identity of mammalian phosphopentomutase has not yet been established unequivocally. That of glucose-1,6-bisphosphate synthase, the enzyme that synthesizes a cofactor for phosphomutases and putative regulator of glycolysis, is completely unknown. In the present work, we have purified phosphopentomutase from human erythrocytes and found it to copurify with a 68-kDa polypeptide that was identified by mass spectrometry as phosphoglucomutase 2 (PGM2), a protein of the ␣-D-phosphohexomutase family and sharing about 20% identity with mammalian phosphoglucomutase 1. Data base searches indicated that vertebrate genomes contained, in addition to PGM2, a homologue (PGM2L1, for PGM2-like 1) sharing about 60% sequence identity with this protein. Both PGM2 and PGM2L1 were overexpressed in Escherichia coli, purified, and their properties were studied. Using catalytic efficiency as a criterion, PGM2 acted more than 10-fold better as a phosphopentomutase (both on deoxyribose 1-phosphate and on ribose 1-phosphate) than as a phosphoglucomutase. PGM2L1 showed only low (<5%) phosphopentomutase and phosphoglucomutase activities compared with PGM2, but was about 5-20-fold better than the latter enzyme in catalyzing the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldosebisphosphates. Furthermore, quantitative real-time PCR analysis indicated that PGM2L1 was mainly expressed in brain where glucose-1,6-bisphosphate synthase activity was previously shown to be particularly high. We conclude that mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase correspond to two closely related proteins, PGM2 and PGM2L1, encoded by two genes that separated early in vertebrate evolution.Phosphopentomutase catalyzes the conversion of the nucleoside breakdown products ribose 1-phosphate and deoxyribose 1-phosphate to the corresponding 5-phosphopentoses. Most bacterial phosphopentomutases characterized so far belong to the same protein family as alkaline phosphatases, sulfatases, and cofactor-independent bisphosphoglycerate mutases (1), though the enzyme from Thermococcus kodakaraensis belongs to the same protein family as mammalian phosphoglucomutase 1 (PGM1), 5 the enzyme that catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate (2).The molecular identity of the mammalian phosphopentomutase is still not ascertained. Biochemical characterization of phosphoglucomutase (PGM) isozymes indicated that one of them, designated PGM2 in man (PGM1 in mouse) was more active as a phosphopentomutase than as a phosphoglucomutase, whereas mammalian PGM1 (equivalent to PGM2 in mouse) has a phosphopentomutase activity representing only about 0.2% of its phosphoglucomutase activity (3). Phosphopentomutase has been purified from rat liver to near homogeneity and shown to coelute with a polypeptide of 32.5 kDa (4), the sequence of which was not determined. Analysis of cell hybrids indicated that the PGM2 locus is on human chromosome 4p14-q12 (5). A putative protein sharing Ϸ20% identit...

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Presence of a Novel Phosphopentomutase and a 2-Deoxyribose 5-Phosphate Aldolase Reveals a Metabolic Link between Pentoses and Central Carbon Metabolism in the Hyperthermophilic Archaeon Thermococcus kodakaraensis

Cited by 50 publications

References 31 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

Purine and pyrimidine nucleotide metabolism in Mollicutes

Molecular Identification of Mammalian Phosphopentomutase and Glucose-1,6-bisphosphate Synthase, Two Members of the α-D-Phosphohexomutase Family

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