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2.6.1.39: 2-aminoadipate transaminase

This is an abbreviated version!
For detailed information about 2-aminoadipate transaminase, go to the full flat file.

Word Map on EC 2.6.1.39

Reaction

L-2-aminoadipate
+
2-oxoglutarate
=
2-oxoadipate
+
L-glutamate

Synonyms

2-aminoadipate aminotransferase, 2-aminoadipic aminotransferase, AAA-AT, AadAT, AAT, alpha-aminoadipate aminotransferase, alpha-aminoadipate aminotransferase (gene aro8), aminoadipate aminotransferase, aminoadipate aminotransferase/kynurenine aminotransferase II, Aro8, GKAT, glutamate-alpha-ketoadipate transaminase, glutamic-ketoadipic transaminase, halogenated tyrosine aminotransferase, KAT II/AADAT, kynurenine aminotransferase II, kynurenine aminotransferase II (EC 2.6.1.7), kynurenine/alpha-aminoadipate aminotransferase, More

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.39 2-aminoadipate transaminase

Crystallization

Crystallization on EC 2.6.1.39 - 2-aminoadipate transaminase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
complexed with N-(5'-phosphopyridoxyl)-L-glutamate, vapor diffusion method, using 16% (w/v) PEG3350, 100 mM HEPES, pH 7.0, and 200 mM calcium acetate, at 20°C
crystal structures of AAA-AT in four forms: with pyridoxal 5'-phosphate (PLP) (PLP complex), with PLP and leucine (PLP/Leu complex), with N-phosphopyridoxyl-leucine (PPL) (PPL complex), and with N-phosphopyridoxyl-alpha-aminoadipate (PPA) at 2.67, 2.26, 1.75, and 1.67 A resolution, respectively
-
in complex with pyridoxal 5'-phosphate, with pyridoxal 5'-phosphate and leucine, with N-phosphopyridoxyl-leucine, and with N-phosphopyridoxyl-alpha-aminoadipate, at 2.67, 2.26, 1.75 and 1.67 A resolution, respectively. Enzyme contains a mobile alpha2-helix involved in substrate recognition
-