Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Homo sapiens |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
isoform KAT II | - |
Purification (Comment) | Organism |
---|---|
recombinant protein | Homo sapiens |