[6] Triose-phosphate isomerase from Pyrococcus woesei and Methanothermus fervidus

Schramm, Alexander; Kohlhoff, Michael; Hensel, Reinhard

doi:10.1016/s0076-6879(01)31047-9

Cited by 10 publications

(9 citation statements)

References 34 publications

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“…C below the physiological optimum, in order to avoid rapid heat-destruction of the labile substrates. 22 The K m values for DHAP and GAP (calculated for the reactive (unhydrated) substrate, Figure 3. The graph shows the nature of the exposed surface area in each classical TIM dimer.…”

Section: Oligomerisation State Of Ttxtim Under Nondenaturing Conditionsmentioning

confidence: 99%

“…22 The PCR product comprising 450 bp was cloned in E. coli TOP10 using pCR-TOPO 2.1 as the vector. For hybridization, the PCR product was labeled using the DIG High Prime Kit, according to the manufacturer's instructions (Roche).…”

Section: Purification Of Tim From T Tenax Cellsmentioning

confidence: 99%

“…1,4 Whereas eucaryal, bacterial and archaeal TIMs adapted to lower temperatures are homodimers, the hyperthermophilic TIMs are tetrameric. 21,22 The TIM of T. maritima (TmTIM) exists as a bifunctional fusion protein in vivo, with the N terminus of TmTIM linked covalently to the C terminus of 3-phosphoglycerate kinase (PGK). The wild-type protein is tetrameric, comprising four PGK-TIM chains linked covalently through disulphide bonds.…”

Section: Introductionmentioning

confidence: 99%

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Structure and Function of a Regulated Archaeal Triosephosphate Isomerase Adapted to High Temperature

Walden¹,

Taylor²,

Lorentzen³

et al. 2004

Journal of Molecular Biology

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Section: Oligomerisation State Of Ttxtim Under Nondenaturing Conditionsmentioning

confidence: 99%

Section: Purification Of Tim From T Tenax Cellsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Structure and Function of a Regulated Archaeal Triosephosphate Isomerase Adapted to High Temperature

Walden¹,

Taylor²,

Lorentzen³

et al. 2004

Journal of Molecular Biology

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“…However, the enzyme activity is low at temperatures below 40°C, but it is intrinsically stable only up to 75°C [32], which is interesting as growth of M. fervidus may occur up to 97°C [1]. Also, the biochemistry of triose-phosphate isomerase, which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP) in the reversible Embden-Meyerhof-Parnas (EMP) pathway, has been studied to some detail in M. fervidus [34]. …”

Section: Classification and Featuresmentioning

confidence: 99%

Complete genome sequence of Methanothermus fervidus type strain (V24ST)

Anderson

Djao

Misra

et al. 2010

Stand. Genomic Sci.

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Methanothermus fervidus Stetter 1982 is the type strain of the genus Methanothermus. This hyperthermophilic genus is of a thought to be endemic in Icelandic hot springs. M. fervidus was not only the first characterized organism with a maximal growth temperature (97°C) close to the boiling point of water, but also the first archaeon in which a detailed functional analysis of its histone protein was reported and the first one in which the function of 2,3-cyclodiphosphoglycerate in thermoadaptation was characterized. Strain V24ST is of interest because of its very low substrate ranges, it grows only on H2 + CO2. This is the first completed genome sequence of the family Methanothermaceae. Here we describe the features of this organism, together with the complete genome sequence and annotation. The 1,243,342 bp long genome with its 1,311 protein-coding and 50 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.

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“…Several factors argue against the assumption that the use of ADP as phosphoryl group donor is the result of metabolic thermoadaptation. (i) Although ATP is less thermostable than ADP (halflives of 115 and 750 min at 90°C, respectively (14)) the half-life of ATP is much higher than for several intermediates of the EMP pathway such as phosphoenolpyruvate, glyceraldehyde 3-phosphate, or 1,3-bisphosphoglycerate (with half-lives of 6 min at 90°C (36), 3.4 min at 80°C (64), and 1.6 min at 60°C, respectively). 3 Therefore, the thermostability of ATP should not represent the bottleneck for thermoadaptation.…”

Section: Influence Of Metabolites On Hexokinase Activity and Physiolomentioning

confidence: 99%

The Hexokinase of the Hyperthermophile Thermoproteus tenax

Dörr

Zaparty

Tjaden

et al. 2003

Journal of Biological Chemistry

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The phosphorylation of glucose by different sugar kinases plays an essential role in Archaea because of the absence of a phosphoenolpyruvate-dependent transferase system characteristic for Bacteria. In the genome of the hyperthermophilic Archaeon Thermoproteus tenax a gene was identified with sequence similarity to glucokinases of the so-called ROK family (repressor protein, open reading frame, sugar kinase). The T. tenax enzyme, like the recently described ATP-dependent "glucokinase" from Aeropyrum pernix, shows the typical broad substrate specificity of hexokinases catalyzing not only phosphorylation of glucose but also of other hexoses such as fructose, mannose, or 2-deoxyglucose, and thus both enzymes represent true hexokinases. The T. tenax hexokinase shows strikingly low if at all any regulatory properties and thus fulfills no important control function at the beginning of the variant of the EmbdenMeyerhof-Parnas pathway in T. tenax. Transcript analyses reveal that the hxk gene of T. tenax is cotranscribed with an upstream located orfX, which codes for an 11-kDa protein of unknown function. Growth-dependent studies and promoter analyses suggest that post-transcriptional RNA processing might be involved in the generation of the monocistronic hxk message, which is observed only under heterotrophic growth conditions. Data base searches revealed T. tenax hexokinase homologs in some archaeal, few eukaryal, and many bacterial genomes. Phylogenetic analyses confirm that the archaeal hexokinase is a member of the so-called ROK family, which, however, should be referred to as ROK group because it represents a group within the bacterial glucokinase fructokinase subfamily II of the hexokinase family. Thus, archaeal hexokinases represent a second major group of glucose-phosphorylating enzymes in Archaea beside the recently described archaeal ADP-dependent glucokinases, which were recognized as members of the ribokinase family. The distribution of the two types of sugar kinases, differing in their cosubstrate as well as substrate specificity, within Archaea is discussed on the basis of physiological constraints of the respective organisms.

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[6] Triose-phosphate isomerase from Pyrococcus woesei and Methanothermus fervidus

Cited by 10 publications

References 34 publications

Structure and Function of a Regulated Archaeal Triosephosphate Isomerase Adapted to High Temperature

Structure and Function of a Regulated Archaeal Triosephosphate Isomerase Adapted to High Temperature

Complete genome sequence of Methanothermus fervidus type strain (V24ST)

The Hexokinase of the Hyperthermophile Thermoproteus tenax

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