Literature summary for 2.6.1.39 extracted from

Bulfer, S.L.; Brunzelle, J.S.; Trievel, R.C.
Crystal structure of Saccharomyces cerevisiae Aro8, a putative alpha-aminoadipate aminotransferase (2013), Protein Sci., 22, 1417-1424.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.91 A resolution, and comparison to alpha-aminoadipate aminotransferase LysN from Thermus thermophilus and human kynurenine aminotransferase II. The active site reveals asymmetric cofactor binding with lysine-pyridoxal-5-phosphate bound within the active site of one subunit in the Aro8 homodimer and pyridoxamine phosphate and a HEPES molecule bound to the other subunit. The HEPES buffer molecule binds within the substrate-binding site of Aro8	Saccharomyces cerevisiae

Crystallization (Comment)

Organism

to 1.91 A resolution, and comparison to alpha-aminoadipate aminotransferase LysN from Thermus thermophilus and human kynurenine aminotransferase II. The active site reveals asymmetric cofactor binding with lysine-pyridoxal-5-phosphate bound within the active site of one subunit in the Aro8 homodimer and pyridoxamine phosphate and a HEPES molecule bound to the other subunit. The HEPES buffer molecule binds within the substrate-binding site of Aro8

Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P53090	-	-

Synonyms

Synonyms	Comment	Organism
Aro8	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)