alpha-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus.
@article{Miyazaki2004alphaAminoadipateAF, title={alpha-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus.}, author={Takashi Miyazaki and Junichi Miyazaki and Hisakazu Yamane and Makoto Nishiyama}, journal={Microbiology}, year={2004}, volume={150 Pt 7}, pages={ 2327-34 } }
The extremely thermophilic bacterium Thermus thermophilus HB27 synthesizes lysine through alpha-aminoadipate (AAA). In this study, a T. thermophilus gene encoding the enzyme that catalyses transamination of AAA was cloned as a mammalian kynurenine/AAA aminotransferase (Kat2) gene homologue. A T. thermophilus mutant with disruption of the Kat2 homologue required a longer lag phase for growth and showed slower growth in minimal medium. Furthermore, addition of AAA or lysine shortened the lag…
38 Citations
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The crystal structure of HCS complexed with lysine showed that Lysine is bound to the active site with rearrangement of amino acid residues in the substrate-binding site, which accounts for the competitive inhibition by lysines with α-KG.
Involvement of the arginine repressor in lysine biosynthesis of Thermus thermophilus.
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Results indicate that lysine biosynthesis is regulated by arginine in T. thermophilus, suggesting the involvement of argR in regulation of lysin biosynthesis.
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Gel-filtration chromatography showed that Ph-KAT II exists as a homodimer and exhibited enzymatic activity that catalyzes the transamination of L-kynurenine to produce kynurenic acid.
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Results indicate that CaYer152Cp has a possible role only in aromatic amino acids degradation, in contrast to CaAro8CHp, and demonstrated that this enzyme may use 2-oxoadipate and2-oxoglutarate (2-OG) as amino acceptors.
Crystal Structure of Tetrameric Homoisocitrate Dehydrogenase from an Extreme Thermophile, Thermus thermophilus: Involvement of Hydrophobic Dimer-Dimer Interaction in Extremely High Thermotolerance
- Chemistry, BiologyJournal of bacteriology
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The crystal structure and mutation analysis indicate that tetramer formation is involved in the extremely high thermotolerance of TtHICDH.
Crystal Structure of the LysY·LysW Complex from Thermus thermophilus*
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Structural insights suggest the formation of a TtLysWZY ternary complex, in which the flexible C-terminal extension of Tt LysW promotes the efficient transfer of the labile intermediate from the active site of TTLysZ to that of T tLysY during the sequential reactions catalyzed by Tt lysZY.
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