Structure of an archaeal alanine:glyoxylate aminotransferase

Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):696-9. doi: 10.1107/S0907444908006732. Epub 2008 May 14.


The crystal structure of a novel alanine:glyoxylate aminotransferase from the hyperthermophilic archaeon Thermococcus litoralis was determined at 2.3 A resolution. The asymmetric unit contains four homologous subunits and the functional tetramer is generated by noncrystallographic 222 symmetry. Although the main-chain coordinates of the monomer of the Thermococcus litoralis enzyme showed a high degree of similarity to those of aspartate aminotransferase from Thermus thermophilus HB8, the amino-acid residues involved in substrate binding in the aspartate aminotransferase are only partially conserved in the Thermococcus litoralis enzyme. This may account for the difference in the substrate specificities of the two enzymes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Crystallography, X-Ray
  • Models, Molecular
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Species Specificity
  • Substrate Specificity
  • Thermococcus / enzymology*
  • Thermococcus / genetics
  • Thermus thermophilus / enzymology
  • Thermus thermophilus / genetics
  • Transaminases / chemistry*
  • Transaminases / genetics


  • Recombinant Proteins
  • Transaminases
  • Alanine-glyoxylate transaminase