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B6db references: 18560158

type Journal Article
authors Sakuraba H, Yoneda K, Takeuchi K, Tsuge H, Katunuma N, Ohshima T.
title Structure of an archaeal alanine:glyoxylate aminotransferase
journal Acta Crystallogr D Biol Crystallogr
sel selected
ui 18560158
year (2008)
volume 64
number 6
pages 696-9
abstract 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.
last changed 2009/03/11 13:13

B6db references