A histidine gene cluster of the hyperthermophile Thermotoga maritima: sequence analysis and evolutionary significance

R Thoma, M Schwander, W Liebl, K Kirschner… - Extremophiles, 1998 - Springer
The sequences of histidine operon genes in hyperthermophiles are informative for
understanding high protein thermostability and the evolution of metabolic pathways …

Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate: A comparison with the structure of the …

RK Wierenga, MEM Noble, G Vriend, S Nauche… - Journal of molecular …, 1991 - Elsevier
Triosephosphate isomerase (TIM) is a dimeric glycolytic enzyme. TIM from Trypanosoma
brucei brucei has been crystallized at pH 7.0 in 2.4 m-ammonium sulphate. The well …

Thermal Unfolding of Triosephosphate Isomerase from Entamoeba histolytica: Dimer Dissociation Leads to Extensive Unfolding

LA Tellez, LM Blancas-Mejia, E Carrillo-Nava… - Biochemistry, 2008 - ACS Publications
In mesophiles, triosephosphate isomerase (TIM) is an obligated homodimer. We have
previously shown that monomeric folding intermediates are common in the chemical …

A role for flexible loops in enzyme catalysis

MM Malabanan, TL Amyes, JP Richard - Current opinion in structural …, 2010 - Elsevier
Triosephosphate isomerase (TIM), glycerol 3-phosphate dehydrogenase, and orotidine 5′-
monophosphate decarboxylase each use the binding energy from the interaction of …

Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: insights into the secondary structure of the stable equilibrium intermediates by …

T Rojsajjakul, P Wintrode, R Vadrevu… - Journal of molecular …, 2004 - Elsevier
The urea-induced unfolding of the α subunit of tryptophan synthase (αTS) from Escherichia
coli, an eight-stranded (β/α) 8 TIM barrel protein, has been shown to involve two stable …

The critical role of the loops of triosephosphate isomerase for its oligomerization, dynamics, and functionality

AR Katebi, RL Jernigan - Protein Science, 2014 - Wiley Online Library
Triosephosphate isomerase (TIM) catalyzes the reaction to convert dihydroxyacetone
phosphate into glyceraldehyde 3‐phosphate, and vice versa. In most organisms, its …

The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy

C Liebold, F List, HR Kalbitzer, R Sterner… - Protein …, 2010 - Wiley Online Library
The imidazole glycerol phosphate (ImGP) synthase from the hyperthermophilic bacterium
Thermotoga maritima is a 1: 1 complex of the glutaminase subunit HisH and the cyclase …

Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus

PG Varley, RH Pain - Journal of molecular biology, 1991 - Elsevier
Phosphoglycerate kinases from yeast and the extreme thermophilic bacterium Thermus
thermophilus HB8 have been used as models for investigating the relationship between …

Stabilisation of a (βα) 8-barrel protein designed from identical half barrels

T Seitz, M Bocola, J Claren, R Sterner - Journal of molecular biology, 2007 - Elsevier
It has been suggested that the common (βα) 8-barrel enzyme fold has evolved by the
duplication and fusion of identical (βα) 4-half barrels, followed by the optimisation of their …

Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria: structural comparison of the predicted protein …

F Rentier-Delrue, SC Mande, S Moyens… - Journal of molecular …, 1993 - Elsevier
We focused on the temperature adaptation of triosephosphate isomerase (TIM; EC 5.3. 1.1.)
by comparing the structure of TIMs isolated from bacterial organisms living in either cold or …