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Literature summary for 2.6.1.7 extracted from

  • Rossi, F.; Garavaglia, S.; Montalbano, V.; Walsh, M.A.; Rizzi, M.
    Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia (2008), J. Biol. Chem., 283, 3559-3566.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isoform KAT II
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Homo sapiens