1bjw

Structural highlights

Function

AAPAT_THET8 Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637). Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275).^{[1] [2] [3]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Aspartate aminotransferase 3D structures

References

1. ↑ Dornfeld C, Weisberg AJ, K C R, Dudareva N, Jelesko JG, Maeda HA. Phylobiochemical characterization of class-Ib aspartate/prephenate aminotransferases reveals evolution of the plant arogenate phenylalanine pathway. Plant Cell. 2014 Jul;26(7):3101-14. PMID:25070637 doi:10.1105/tpc.114.127407
2. ↑ Giustini C, Graindorge M, Cobessi D, Crouzy S, Robin A, Curien G, Matringe M. Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase. FEBS J. 2019 Feb 16. doi: 10.1111/febs.14789. PMID:30771275 doi:http://dx.doi.org/10.1111/febs.14789
3. ↑ Okamoto A, Kato R, Masui R, Yamagishi A, Oshima T, Kuramitsu S. An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. J Biochem. 1996 Jan;119(1):135-44. PMID:8907187 doi:10.1093/oxfordjournals.jbchem.a021198