2zg5

From Proteopedia

Revision as of 11:26, 5 March 2008

Crystal structure of LysN, alpha-aminoadipate aminotransferase (Leucine complex), 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

2ZG5 is a Single protein structure of sequence from Thermus thermophilus with as ligand. This structure supersedes the now removed PDB entry 2DTV. Active as 2-aminoadipate transaminase, with EC number 2.6.1.39 Known structural/functional Sites: , and . 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

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