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Literature summary for 2.6.1.1 extracted from

  • Arnone, M.I.; Birolo, L.; Pascarella, S.; Cubellis, M.V.; Bossa, F.; Sannia, G.; Marino, G.
    Stability of aspartate aminotransferase from Sulfolobus solfataricus. (1997), Protein Eng., 10, 237-248.
    View publication on PubMed
Search for more literature for 2.6.1.1

Organic Solvent Stability

Organic Solvent Comment Organism
guanidine-HCl 4.0-6.0 M, 1 h, complete denaturation. SsAspAT is fully unfolded in the presence of denaturant concentrations higher than 3.5 M Saccharolobus solfataricus
guanidine-HCl at 25°C, the enzyme from Sulfolobus solfataricus is less resistant to guanidinium chloride-induced denaturation than the cytosolic mesophilic aspartate aminotransferase from pig heart Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-
Saccharolobus solfataricus P14909
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus
recombinant protein Saccharolobus solfataricus

Renatured (Commentary)

Renatured (Comment) Organism
refolding of SsAspAT can be accelerated by increasing the temperature from 25 to 50°C. Although refolding is faster at 50°C (35% of native enzyme) the highest yield of renaturation is obtained at 37°C (70% reactivation), similar to the yield of 65% of initial activity that is obtained at 25°C Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine sulfinic acid + 2-oxoglutarate
-
 Saccharolobus solfataricus 2-oxo-3-sulfinopropionic acid + L-glutamate
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
aspartate aminotransferase
-
 Saccharolobus solfataricus
SsAspAT
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
100
-
-
 Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 structural stability of the enzyme is investigated by coupling isothermally and thermally induced denaturation studies to molecular modeling. Gel filtration analysis indicates that the enzyme unfolds with an N2 reversible 2D mechanism. In the molecular model, a cluster of hydrophobic residues is shown at the interface between the subunits of the enzyme and suggests this cluster as a structural feature stabilizing the enzyme quaternary structure Saccharolobus solfataricus
100
-
 the enzyme retains its structure at 100°C Saccharolobus solfataricus