Literature summary for 2.6.1.1 extracted from

Arnone, M.I.; Birolo, L.; Giamberini, M.; Cubellis, M.V.; Nitti, G.; Sannia, G.; Marino, G.
Limited proteolysis as a probe of conformational changes in aspartate aminotransferase from Sulfolobus solfataricus. (1992), Eur. J. Biochem., 204, 1183-1189.

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General Stability

General Stability	Organism
AspATSs, when incubated at 37°C in the presence of trypsin, is cleaved after Lys32 and Lys33 and looses its activity. At 37°C, substrates are not able to protect the enzyme from proteolysis, while at 75°C the presence of substrates lowers the inactivation rate about 4fold	Saccharolobus solfataricus
presence of substrates renders AspATSs less sensitive to thermolysin, possibly by inducing a conformational transition	Saccharolobus solfataricus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	P14909	-	-

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	-	?

Synonyms

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

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Release 2023.1 (January 2023)