Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.2.1.13	overexpression in Escherichia coli	Saccharolobus solfataricus

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.2.1.13	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

EC Number	Organism	UniProt	Comment	Textmining
1.2.1.13	Saccharolobus solfataricus	P39460	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.2.1.13	-	Saccharolobus solfataricus

Synonyms

EC Number	Synonyms	Comment	Organism
1.2.1.13	GAPDH	-	Saccharolobus solfataricus

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
1.2.1.13	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

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Release 2023.1 (January 2023)