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Literature summary extracted from

  • Park, S.H.; Kim, H.S.; Park, M.S.; Moon, S.; Song, M.K.; Park, H.S.; Hahn, H.; Kim, S.J.; Bae, E.; Kim, H.J.; Han, B.W.
    Structure and stability of the dimeric triosephosphate isomerase from the thermophilic archaeon Thermoplasma acidophilum (2015), PLoS ONE, 10, e0145331 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.1 structures of apo- and glycerol-3-phosphate-bound TPI, to 1.94 and 2.17 A resolution, respectively. The protein adopts the canonical TIM-barrel fold with eight alpha-helices and parallel eight beta-strands Thermoplasma acidophilum

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.1 Thermoplasma acidophilum Q9HLB6
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-
5.3.1.1 Thermoplasma acidophilum DSM 17280 Q9HLB6
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-

Synonyms

EC Number Synonyms Comment Organism
5.3.1.1 TpiA
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 Thermoplasma acidophilum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.1.1 74.6
-
 half-denaturation temperature Thermoplasma acidophilum

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
5.3.1.1 additional information
-
 enzyme maintains its overall structure with some changes in the secondary structure contents at pH 1-2 Thermoplasma acidophilum