3PD6

Crystal structure of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV

Summary for 3PD6

• Entry DOI: 10.2210/pdb3pd6/pdb
• Related: 3PDB
• Descriptor: Aspartate aminotransferase, mitochondrial, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, GLYCEROL, ... (6 entities in total)
• Functional Keywords: alpha & beta protein, aminotransferase, plp-binding, mitochondrion, transferase
• Biological source: Mus musculus (mouse); More
• Cellular location: Mitochondrion matrix: P05202 P05202
• Total number of polymer chains: 4
• Total formula weight: 180909.92

Authors

Han, Q.,Robinson, H.,Cai, T.,Tagle, D.A.,Li, J. (deposition date: 2010-10-22, release date: 2010-11-10, Last modification date: 2023-12-06)

Primary citation

Han, Q.,Robinson, H.,Cai, T.,Tagle, D.A.,Li, J.
Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV.
Biosci.Rep., 31:323-332, 2011

PubMed Abstract: Mammalian mAspAT (mitochondrial aspartate aminotransferase) is recently reported to have KAT (kynurenine aminotransferase) activity and plays a role in the biosynthesis of KYNA (kynurenic acid) in rat, mouse and human brains. This study concerns the biochemical and structural characterization of mouse mAspAT. In this study, mouse mAspAT cDNA was amplified from mouse brain first stand cDNA and its recombinant protein was expressed in an Escherichia coli expression system. Sixteen oxo acids were tested for the co-substrate specificity of mouse mAspAT and 14 of them were shown to be capable of serving as co-substrates for the enzyme. Structural analysis of mAspAT by macromolecular crystallography revealed that the cofactor-binding residues of mAspAT are similar to those of other KATs. The substrate-binding residues of mAspAT are slightly different from those of other KATs. Our results provide a biochemical and structural basis towards understanding the overall physiological role of mAspAT in vivo and insight into controlling the levels of endogenous KYNA through modulation of the enzyme in the mouse brain.

PubMed: 20977429
DOI: 10.1042/BSR20100117

Experimental method

X-RAY DIFFRACTION (2.4 Å)