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2.6.1.7: kynurenine-oxoglutarate transaminase

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

Word Map on EC 2.6.1.7

Reaction

L-kynurenine
+
2-oxoglutarate
=
4-(2-aminophenyl)-2,4-dioxobutanoate
 +
L-glutamate

Synonyms

AadAT, aminoadipate aminotransferase, aminotransferase, kynurenine, aspartate aminotransferase, Bna3, CCBL2, cysteine conjugate beta-lyase 1, cysteine conjugate beta-lyase 2, glutamic-oxaloacetic transaminase 2, glutamine transaminase K, KAT, KAT I, KAT II, KAT III, KAT IV, KAT-1, KAT-I, KAT-II, KAT2, KAT3, KAT3/GTL/CCBL2, KYAT3, kynurenine 2-oxoglutarate transaminase, kynurenine aminotransferase, kynurenine aminotransferase 2, kynurenine aminotransferase 3, kynurenine aminotransferase I, kynurenine aminotransferase II, kynurenine aminotransferase III, kynurenine aminotransferase IV, kynurenine aminotransferase-1, kynurenine aminotransferase-I, kynurenine aminotransferase-IV, kynurenine aminotransferases I, kynurenine aminotransferases II, kynurenine pyruvate aminotransferase, kynurenine transaminase (cyclizing), kynurenine-2-oxoglutarate aminotransferase, kynurenine/alpha-aminoadipate aminotransferase, L-kynurenine aminotransferase, mitochondrial aspartate aminotransferase, More, PhKAT, phKAT-II, type II kynurenine aminotransferase

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.7 kynurenine-oxoglutarate transaminase

Crystallization

Crystallization on EC 2.6.1.7 - kynurenine-oxoglutarate transaminase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with its best amino acid substrates, glutamine and cysteine. Glutamine is found in both subunits of the biological dimer, and cysteine is found in one of the two subunits. Both substrates form external aldemines with pyridoxal 5'-phosphate in the structures. All the units with substrate are in the closed conformation form, and the unit without substrate is in the open form. Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does
-
-
Hansenula schneggii
-
5’-pyridoxal phosphate and pyridoxamine form and in complex with competing substrate L-phenylalanine
Comparison of the active site residues of the Aedes aegypti enzyme-cysteine structure with those of the human isoform KAT I-phenylalanine structure reveals that Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes aegypti enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does
-
full-length pyridoxal phosphate-form, to 1.83 A resolution. The electron density of the active site reveals an aldimine linkage between pyridoxal phosphate and Lys263
in complex with 3-indolepropionic acid or DL-indole-3-lactic acid, hanging drop vapor diffusion method, using 22% (w/v) PEG 4000, 0.2 M sodium acetate, 0.1 M Tris, pH 8.5
in complex with pyridoxal 5'-phosphate and aminooxyacetate, hanging drop vapor diffusion method, using 200 mM sodium acetate, 29% (w/v) PEG4000 in 100 mM Tris, pH 7.3
KAT II complex with 2-oxoglutarate, hanging drop vapor diffusion method
native enzyme and selenomethionine derivative, diffraction to 2.3 A and 2.4 A resolution, respectively. Structure reveals an antiparallel strand-loopstrand motif that forms an unprecedented intersubunit beta-sheet in the functional KAT II dimer. The N-terminal regions of KAT II and aspartate aminotransferase appear to have converged to highly similar although 2fold symmetry-related conformations, which fulfill the same functional role. Structural comparison of isoforms KAT I and KAT II reveals a larger and more aliphatic character to the active site of KAT II due to the absence of the aromatic cage involved in ligand binding in KAT I
-
native enzyme, diffraction to 2.16 A resolution, in complex with kynurenine, diffraction to 1.95 A. Enzyme belongs to the fold-type I pyridoxal 5'-phosphate-dependent enzymes and shows a unique folding of its first 65 N-terminal residues
to 1.83 A resolution, space group P43212, with unit cell parameters a = b = 102.46 A, c = 86.24 A, alpha = beta= gamma = 90°
hanging-drop vapor diffusion method, PEG 4000,
in complex with L-kynurenine and L-glutamine, hanging drop vapor diffusion method, using 21% (w/v) polyethylene glycol 400, 10% glycerol, 150 mM CaCl2, and 100 mM HEPES, pH 7.5
monomer structure model of phKAT-II is refined at a resolution of 2.20 A. A single molecule of phKAT-II is present in an asymmetric unit of the crystal
-
sitting-drop vapor diffusion method
-
the crystal structure of the enzyme in complex with pyridoxamine phosphates, kynurenine and kynurenic acid, 1.85 A resolution
diffraction to 2.0 A resolution, comparison with crystallization data from Aspergillus fumigatus, Dictyostelium discoideum, Aedes aegypti, Trypanosoma brucei, Rattus norvegicus, and Homo sapiens