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Therapeutic Targeting of Cancer Metabolism with Triosephosphate Isomerase

Chemistry & Biodiversity, 2020
The increase in glycolytic flux in cancer, known as aerobic glycolysis, is one of the most important hallmarks of cancer. Therefore, glycolytic enzymes have importance in understanding the molecular mechanism of cancer progression.
Gonca Pekel, F. Arı
semanticscholar   +5 more sources

Cold Adaptation of Triosephosphate Isomerase.

Biochemistry, 2017
The main problem for enzymes from psychrophilic species, which need to work near the freezing point of liquid water, is the exponential decay of reaction rates as the temperature is decreased. Cold-adapted enzymes have solved this problem by shifting the
J. Åqvist
semanticscholar   +4 more sources

Proton Transfer in the Mechanism of Triosephosphate Isomerase

Biochemistry, 1998
Triosephosphate isomerase (TIM) catalyzes the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP), with Glu-165 removing the pro-R proton from C1 of DHAP and neutral His-95 polarizing the carbonyl group of the substrate.
Thomas K. Harris   +3 more
openaire   +3 more sources

The Folding Pathway of Triosephosphate Isomerase

2008
Publisher Summary This chapter discusses the folding pathway of triosephosphate isomerase (TIM), which is a widely studied enzyme. The ubiquity, efficient catalytic activity, and (β/α)8 barrel three-dimensional conformation of this enzyme makes it an excellent model to perform almost any kind of research. TIM is a glycolytic enzyme that catalyzes the
Francisco Zarate-Perez   +3 more
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In vitro deamidation of human triosephosphate isomerase

Archives of Biochemistry and Biophysics, 1986
The effects of pH, temperature, buffer ion, ionic strength, protein concentration, and substrate on the rates of specific, spontaneous deamidations of Asn-15 and Asn-71 of human triosephosphate isomerase were examined. Elevated temperature and pH facilitate the deamidations, and the deamidation rate is dependent on the specific buffer ions indicating a
K. Ümit Yüksel, Robert W. Gracy
openaire   +3 more sources

The determination of triosephosphate isomerase

Archives of Biochemistry and Biophysics, 1956
Abstract The difference in rate of formation of the chromogenic 2,4-dinitrophenylosazone derivatives of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate permits accurate measurement of the two triose phosphates in a mixture by means of carefully timed chromogen development reactions.
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Detection of Triosephosphate Isomerase after Electrophoresis [PDF]

open access: possibleNature, 1964
BY coupling enzymes to the reduction of a tetrazolium salt, dehydrogenases can be located on electrophoresis strips, and several have been shown to consist of more than one protein component1,2. It is possible to detect other enzymes if their action leads to the formation of a compound which can be oxidized by a suitable enzyme in the incubation ...
openaire   +2 more sources

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