RT Journal Article SR Electronic(1) A1 Miyazaki, Takashi A1 Miyazaki, Junichi A1 Yamane, Hisakazu A1 Nishiyama, MakotoYR 2004 T1 α-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus JF Microbiology, VO 150 IS 7 SP 2327 OP 2334 DO https://doi.org/10.1099/mic.0.27037-0 PB Microbiology Society, SN 1465-2080, AB The extremely thermophilic bacterium Thermus thermophilus HB27 synthesizes lysine through α-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 phase and improved the growth rate. The Kat2 homologue was therefore termed lysN. LysN recognizes not only 2-oxoadipate, an intermediate of lysine biosynthesis, but also 2-oxoisocaproate, 2-oxoisovalerate and 2-oxo-3-methylvalerate, intermediates of leucine, valine and isoleucine biosyntheses, respectively, along with oxaloacetate, a compound in the TCA cycle, as an amino acceptor. These results suggest multiple roles of LysN in several cellular metabolic pathways including lysine and branched-chain amino acid biosyntheses., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.27037-0