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… 
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The reconstituted conversion of AAA to lysine was found and it was found that the amino group of AAA is modified by attachment to the gamma-carboxyl group of the C-terminal Glu54 of a small protein, LysW, indicating that LysW acts as a carrier protein or protein scaffold for the biosynthetic enzymes.
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The experimental results are compared with bioinformatics data to better understand the amino acid biosynthesis capabilities of this fascinating organism.
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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.
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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.
Overproduction and preliminary crystallographic study of a human kynurenine aminotransferase II homologue from Pyrococcus horikoshii OT3.
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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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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*
TLDR
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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