Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

Kohlhoff, Michael; Dahm, A.; Hensel, Reinhard

doi:10.1016/0014-5793(96)00249-9

Cited by 87 publications

(49 citation statements)

References 32 publications

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“…When the enzyme was passed through a column of Sephacryl S 300 at a concentration of 2.4 mg/ml, it eluted as a protein with a Stokes radius that corsesponded to a protein of 50 kDa. Taken together, these findings indicate that like all the described triosephosphate isomerases, except that of hyperthermopilic Archaea which is a tetramer [23], triosephosphate isomerase from 7: cruzi is a homodimer. The CD spectra of triosephosphate isomerase from 7: cruzi and 7: brucei were almost indistinguishable.…”

Section: Characteristics Of Triosephosphate Isomerase From T Cruzisupporting

confidence: 62%

Cloning, Expression, Purification and Characterization Of Triosephosphate Isomerase from Trypanosoma Cruzi

Ostoa‐Saloma

Garza‐Ramos

Ramı́rez

et al. 1997

European Journal of Biochemistry

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The gene that encodes for triosephosphate isomerase froin Trypanosoma cruzi was cloned and sequenced. In 7: cruzi, there is only one gene for triosephosphate isomerase. The enzyme has an identity of 12% and 68 5% with triosephosphate isomerase from Trypanosoma brucei and Leishmania mexicanu, respectively. The active site residues are conserved: out of the 32 residues that conform the interface of dimeric triosephosphate isomerase from 7: brucei, 29 are conserved in the 7: cruzi enzyme. The enzyme was expressed in Escherichia coli and purified to homogeneity. Data from electrophoretic analysis under denaturing techniques and filtration techniques showed that triosephosphate isomerase from 7: cruzi is a homodimer. Some of its structural and kinetic features were determined and compared to those of the purified enzymes from 7: brucei and L. mexicana. Its circular dichroism spectrum was almost identical to that of triosephosphate isomerase from 7: brucei. Its kinetic properties and pH optima were similar to those of ' I: brucei and L. mexicana, although the latter exhibited a higher V,,,, with glyceraldehyde 3-phosphate as substrate. The sensitivity of the three enzymes to the sulfhydryl reagent methylmethane thiosulfonate (MeS0,-SMe) was determined; the sensitivity of the 7: cruzi enzyme was about 40 times and 200 times higher than that of the enzymes from 7: brucei and L. mexicana, respectively. Triosephosphate isomerase from 7: cruzi and L. mexicana have the three cysteine residues that exist in the ' I : brucei enzyme (positiuns 14, 39, 126, using the numbering of the 7: brucei enzyme); however, they also have an additional residue (position 1 1 7). These data suggest that regardless of the high identity of the three trypanosomatid enzymes, there are structural differences in the disposition of their cysteine residues that account for their different sensitivity to the sulthydryl reagent. The disposition of the cysteine in triosephosphate isomerase from 7: cr~17i appears to make it unique for inhibition by modification of its cysteine.

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Section: Characteristics Of Triosephosphate Isomerase From T Cruzisupporting

confidence: 62%

Cloning, Expression, Purification and Characterization Of Triosephosphate Isomerase from Trypanosoma Cruzi

Ostoa‐Saloma

Garza‐Ramos

Ramı́rez

et al. 1997

European Journal of Biochemistry

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“…Recent evidence from the prokaryotes might indicate that the latter is at least a possibility and that TPI can function as a tetramer. Two instances of tetrameric TPI, both from hyperthermophilic organisms, have been reported and suggested to represent an adaptation for stability at high growth temperatures (21,24). The TPIs from T. maritima and the related bacterial species T. neopolitana are expressed as tetrameric fusion proteins with PGK (34,44), while the TPI of the hyperthermophilic archaea Methanothermus fervidus and Pyrococcus woesei are tetramers derived from an independent tpi gene (24).…”

Section: Discussionmentioning

confidence: 99%

The tigA gene is a transcriptional fusion of glycolytic genes encoding triose-phosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase in oomycota

Unkles¹,

Logsdon²,

Robison³

et al. 1997

J Bacteriol

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Genes encoding triose-phosphate isomerase (TPI) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are fused and form a single transcriptional unit (tigA) in Phytophthora species, members of the order Pythiales in the phylum Oomycota. This is the first demonstration of glycolytic gene fusion in eukaryotes and the first case of a TPI-GAPDH fusion in any organism. The tigA gene from Phytophthora infestans has a typical Oomycota transcriptional start point consensus sequence and, in common with most Phytophthora genes, has no introns. Furthermore, Southern and PCR analyses suggest that the same organization exists in other closely related genera, such as Pythium, from the same order (Oomycota), as well as more distantly related genera, Saprolegnia and Achlya, in the order Saprolegniales. Evidence is provided that in P. infestans, there is at least one other discrete copy of a GAPDH-encoding gene but not of a TPI-encoding gene. Finally, a phylogenetic analysis of TPI does not place Phytophthora within the assemblage of crown eukaryotes and suggests TPI may not be particularly useful for resolving relationships among major eukaryotic groups.The enzymes triose-phosphate isomerase (TPI) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyze sequential steps in the major pathways of carbohydrate metabolism, including glycolysis and gluconeogenesis. GAPDH catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate following its isomerization from dihydroxyacetone phosphate by TPI. In all organisms studied thus far, GAPDH is a tetrameric protein, which is homomeric (EC 1.2

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“…TIM activity has been detected in crude extracts of many archaeal species (40-42, 70, 105, 128), and TIM sequences have been identified in apparently all archaeal genomes (36,43 (145)(146)(147)(148). The archaeal TIM sequences are shorter, by ϳ20 amino acids, than those of their bacterial/eukaryotic counterparts, comprising ϳ230 amino acids and ϳ250 to 260 amino acids, corresponding to ϳ24 kDa and 28 kDa, respectively (36,139). The characterized hyperthermophilic archaeal TIM proteins represent homotetramers, whereas the mesophilic TIMs from Bacteria and Eukarya are homodimers.…”

Section: Triosephosphate Isomerasementioning

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

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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Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

Cited by 87 publications

References 32 publications

Cloning, Expression, Purification and Characterization Of Triosephosphate Isomerase from Trypanosoma Cruzi

Cloning, Expression, Purification and Characterization Of Triosephosphate Isomerase from Trypanosoma Cruzi

The tigA gene is a transcriptional fusion of glycolytic genes encoding triose-phosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase in oomycota

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

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