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Updated: Jul 15, 2026

Assaying the Kinase Activity of LRRK2 in vitro
Published on: January 18, 2012
Phylogenetic and disruption analyses of aspartate kinase of Deinococcus radiodurans
1Agricultural Bioinformatics Research Unit, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo, Japan. hnishida@iu.a.u-tokyo.ac.jp
Abstract:
The extremely radioresistant bacterium Deinococcus radiodurans is evolutionarily closely related to the extremely thermophilic bacterium Thermus thermophilus. These bacteria have a single gene encoding an aspartate kinase (AK) that catalyzes the phosphorylation of L-aspartate. T. thermophilus has an aminoadipate pathway for lysine biosynthesis that does not use AK for lysine biosynthesis. Phylogenetic analysis in this study indicated that D. radiodurans AK has a different protein structure and a different evolutionary history from T. thermophilus AK. Disruption analysis of D. radiodurans AK indicated that D. radiodurans AK was not used for lysine biosynthesis but for threonine and methionine biosyntheses. A D. radiodurans AK disruption mutant exhibited a phenotype similar to a T. thermophilus AK disruption mutant, which indicates that these two AKs have different evolutionary origins, though their functions are not different.
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