Triose-phosphate isomerase from Pyrococcus woesei and Methanothermus fervidus

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Abstract

Triose-phosphate isomerase (TIM) catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3- phosphate (GAP) in the reversible Embden-Meyerhof–Parnas (EMP) pathway. It represents one of the most thoroughly investigated enzymes. More than 40 amino acid sequences mainly deduced from the coding genes of bacteria and eukarya are deposited at data banks. The three-dimensional structures of at least one bacterial and seven eukaryal enzymes have been solved. All bacterial and eukaryal TIMs from mesophilic and moderately thermophilic sources are homomeric dimers with a molecular mass of 50-60 kDa. Contrary to the situation with eukaryal and bacterial TIMs, knowledge about archaeal enzymes is rather scarce. Functional and structural information about TIM from hyperthermophilic members of the Archaea would give valuable insights into the molecular basis for thermoadaptation. This article gives methodological and phenotypical information on TIMs of the archaeal hyperthermophiles Pyrococcus woesei (optimal growth temperature: 100 °) and Methanothermus fervidus (optimal growth temperature: 83°).

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Schramm, A., Kohlhoff, M., & Hensel, R. (2001). Triose-phosphate isomerase from Pyrococcus woesei and Methanothermus fervidus. Methods in Enzymology. Academic Press Inc. https://doi.org/10.1016/S0076-6879(01)31047-9

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