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Microbiology 150 (2004), 2327-2334; DOI  10.1099/mic.0.27037-0
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Microbiology 150 (2004), 2327-2334; DOI  10.1099/mic.0.27037-0
© 2004 Society for General Microbiology

{alpha}-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus

Takashi Miyazaki, Junichi Miyazaki, Hisakazu Yamane and Makoto Nishiyama

Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan

Correspondence
Makoto Nishiyama
umanis{at}mail.ecc.u-tokyo.ac.jp

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 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.

Abbreviations: AAA, {alpha}-aminoadipate; AAAAT, {alpha}-aminoadipate aminotransferase; BcAT, branched-chain amino acid aminotransferase; 2-OA, 2-oxoadipate; 2-OIC, 2-oxoisocaproate; 2-OIV, 2-oxoisovalerate; 2-OMV, 2-oxo-3-methylvalerate

The GenBank accession number for the sequence reported in this paper is AB097117.




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