Among Multiple Phosphomannomutase Gene Orthologues, Only One Gene Encodes a Protein with Phosphoglucomutase and Phosphomannomutase Activities in
            <i>Thermococcus kodakaraensis</i>

Rashid, Naeem; Kanai, Tamotsu; Atomi, Haruyuki; Imanaka, Tadayuki

doi:10.1128/jb.186.18.6070-6076.2004

Cited by 32 publications

(47 citation statements)

References 23 publications

(30 reference statements)

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“…Interestingly, Thermococcus kodakaraensis has the genes for M1P-GT/PMI immediately upstream of the phosphomannomutase gene but lacks the mpgS/mpgP cluster (36). In other archaea and bacteria examined, mpgS and mpgP have an adjacent location but the genes encoding M1P-GT/PMI and phosphomannomutase appear elsewhere in the genome (5,11,12).…”

Section: Discussionmentioning

confidence: 99%

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

Neves

Costa

Santos

2005

Appl Environ Microbiol

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The effect of salinity and growth temperature on the accumulation of intracellular organic solutes was examined in the hyperthermophilic archaeon Palaeococcus ferrophilus. The genus Palaeococcus represents a deep-branching lineage of the order Thermococcales, which diverged before Thermococcus and Pyrococcus. Palaeococcus ferrophilus accumulated mannosylglycerate, glutamate, and aspartate as major compatible solutes. Unlike members of the genera Pyrococcus and Thermococcus, Palaeococcus ferrophilus did not accumulate di-myo-inositol phosphate, a canonical solute of hyperthermophiles. The level of mannosylglycerate increased in response to both heat and salt stress; glutamate increased at supraoptimal growth temperatures, whereas aspartate increased at supraoptimal salt concentration. Proline, alanine, and trehalose were also found in lesser amounts, but their levels did not respond significantly to any of the stresses imposed. Additionally, the genes involved in the synthesis of mannosylglycerate in Palaeococcus ferrophilus and Thermococcus litoralis were identified. In both organisms the synthesis proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase (MPGS) (EC 2.4.1.217) and mannosyl-3-phosphoglycerate phosphatase (MPGP) (EC 3.1.3.70). The mpgS and mpgP genes of Palaeococcus ferrophilus were expressed in Escherichia coli and the proteins were characterized. MPGS had maximal activity at 90°C and pH near 7.0, and was strictly dependent on Mg 2؉ . MPGP had optimal activity at 90°C and pH 6.0 and was barely dependent on Mg 2؉ . The half-life values for inactivation of MPGS and MPGP at 83°C were 18 and 25 min, respectively. A comparative discussion of the osmo-and thermoadaptation strategies in these three genera of the Thermococcales is presented.

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Section: Discussionmentioning

confidence: 99%

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

Neves

Costa

Santos

2005

Appl Environ Microbiol

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“…In accordance with this, PGM was induced during growth on starch. PGM from A. fulgidus strain 7324 and T. kodakaraensis constitutes a homotetramer of 49-kDa subunits (52). Thus, both archaeal enzymes differ from their bacterial and eukaryotic counterparts, which appear to be monomeric and dimeric proteins (16,38,58).…”

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confidence: 99%

“…Within the domain of Archaea, PGM activities were found in crude extracts of T. litoralis (72), T. kodakaraensis (52), and Methanococcus maripaludis (74). Respective genes from Thermococcus kodakaraensis and from Pyrococcus horokoshii were heterologously expressed in E. coli and characterized (1,52). As part of the starch degradation pathway, PGM from A. fulgidus catalyzed the conversion of glucose-1-phosphate to glucose-6-phosphate, providing the substrate for the modified EM pathway (30).…”

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confidence: 99%

“…Most PGMs belong to the bifunctional PGM/phosphomannose family (16,36,46,53). Within the domain of Archaea, PGM activities were found in crude extracts of T. litoralis (72), T. kodakaraensis (52), and Methanococcus maripaludis (74). Respective genes from Thermococcus kodakaraensis and from Pyrococcus horokoshii were heterologously expressed in E. coli and characterized (1,52).…”

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confidence: 99%

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Unusual Starch Degradation Pathway via Cyclodextrins in the Hyperthermophilic Sulfate-Reducing Archaeon Archaeoglobus fulgidus Strain 7324

Labes

Schönheit

2007

J Bacteriol

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The hyperthermophilic archaeon Archaeoglobus fulgidus strain 7324 has been shown to grow on starch and sulfate and thus represents the first sulfate reducer able to degrade polymeric sugars. The enzymes involved in starch degradation to glucose 6-phosphate were studied. In extracts of starch-grown cells the activities of the classical starch degradation enzymes, ␣-amylase and amylopullulanase, could not be detected. Instead, evidence is presented here that A. fulgidus utilizes an unusual pathway of starch degradation involving cyclodextrins as intermediates. The pathway comprises the combined action of an extracellular cyclodextrin glucanotransferase (CGTase) converting starch to cyclodextrins and the intracellular conversion of cyclodextrins to glucose 6-phosphate via cyclodextrinase (CDase), maltodextrin phosphorylase (Mal-P), and phosphoglucomutase (PGM). These enzymes, which are all induced after growth on starch, were characterized. CGTase catalyzed the conversion of starch to mainly ␤-cyclodextrin. The gene encoding CGTase was cloned and sequenced and showed highest similarity to a glucanotransferase from Thermococcus litoralis. After transport of the cyclodextrins into the cell by a transport system to be defined, these molecules are linearized via a CDase, catalyzing exclusively the ring opening of the cyclodextrins to the respective maltooligodextrins. These are degraded by a Mal-P to glucose 1-phosphate. Finally, PGM catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate, which is further degraded to pyruvate via the modified Embden-Meyerhof pathway.

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“…However, members of this phosphohexomutase family catalyze the isomerization of different sugar phosphates, making it difficult to predict substrate specificity (34). The previously characterized archaeal homologs from Pyrococcus horikoshii (2), Sulfolobus solfataricus (32), and Thermococcus kodakaraensis (31) have both phosphoglucomutase and phosphomannomutase activities but lack significant phosphoglucosamine phosphomutase activity. Another member of this family, from T. kodakaraensis, has phosphopentomutase activity (30).…”

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confidence: 99%

Acetamido Sugar Biosynthesis in the Euryarchaea

Namboori

Graham

2008

J Bacteriol

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Archaea and eukaryotes share a dolichol phosphate-dependent system for protein N-glycosylation. In both domains, the acetamido sugar N-acetylglucosamine (GlcNAc) forms part of the core oligosaccharide. However, the archaeal Methanococcales produce GlcNAc using the bacterial biosynthetic pathway. Key enzymes in this pathway belong to large families of proteins with diverse functions; therefore, the archaeal enzymes could not be identified solely using comparative sequence analysis. Genes encoding acetamido sugar-biosynthetic proteins were identified in Methanococcus maripaludis using phylogenetic and gene cluster analyses. Proteins expressed in Escherichia coli were purified and assayed for the predicted activities. The MMP1680 protein encodes a universally conserved glucosamine-6-phosphate synthase. The MMP1077 phosphomutase converted ␣-D-glucosamine-6-phosphate to ␣-D-glucosamine-1-phosphate, although this protein is more closely related to archaeal pentose and glucose phosphomutases than to bacterial glucosamine phosphomutases. The thermostable MJ1101 protein catalyzed both the acetylation of glucosamine-1-phosphate and the uridylyltransferase reaction with UTP to produce UDP-GlcNAc. The MMP0705 protein catalyzed the C-2 epimerization of UDP-GlcNAc, and the MMP0706 protein used NAD ؉ to oxidize UDP-N-acetylmannosamine, forming UDP-N-acetylmannosaminuronate (ManNAcA). These two proteins are similar to enzymes used for proteobacterial lipopolysaccharide biosynthesis and gram-positive bacterial capsule production, suggesting a common evolutionary origin and a widespread distribution of ManNAcA. UDP-GlcNAc and UDP-ManNAcA biosynthesis evolved early in the euryarchaeal lineage, because most of their genomes contain orthologs of the five genes characterized here. These UDP-acetamido sugars are predicted to be precursors for flagellin and S-layer protein modifications and for the biosynthesis of methanogenic coenzyme B.

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Among Multiple Phosphomannomutase Gene Orthologues, Only One Gene Encodes a Protein with Phosphoglucomutase and Phosphomannomutase Activities in Thermococcus kodakaraensis

Cited by 32 publications

References 23 publications

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

Unusual Starch Degradation Pathway via Cyclodextrins in the Hyperthermophilic Sulfate-Reducing Archaeon Archaeoglobus fulgidus Strain 7324

Acetamido Sugar Biosynthesis in the Euryarchaea

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