2z1y
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Revision as of 06:53, 4 June 2008
Crystal structure of LysN, alpha-aminoadipate aminotransferase (complexed with N-(5'-phosphopyridoxyl)-L-leucine), from Thermus thermophilus HB27
Overview
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.
About this Structure
2Z1Y is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
alpha-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus., Miyazaki T, Miyazaki J, Yamane H, Nishiyama M, Microbiology. 2004 Jul;150(Pt 7):2327-34. PMID:15256574 Page seeded by OCA on Wed Jun 4 09:53:33 2008
