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Literature summary for 1.2.1.13 extracted from

  • Isupov, M.N.; Fleming, T.M.; Dalby, A.R.; Crowhurst, G.S.; Bourne, P.C.; Littlechild, J.A.
    Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus (1999), J. Mol. Biol., 291, 651-660.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
determination of the crystal structure of the apoenzyme by multiple isomorphous replacement at 2.05 A resolution, hanging drop technique. The crystals belong to space group P4(1)2(1)2 or its enantiomorph with cell dimensions a = b = 102.3 A, c = 181.6 A, which contract upon cryocooling at 100 K to a = b = 101.6 A, c = 179.9 A. The asymmetric unit contains two subunits with a molecular mass of 37611 Da Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus P39460
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
GAPDH
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Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
activity half-life: 17 h. The thermostability of the enzyme can be attributed to a combination of an ion pair cluster and an intrasubunit disulfide bond Saccharolobus solfataricus