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2dtv

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(New page: 200px<br /><applet load="2dtv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2dtv, resolution 2.26&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: thermus thermophilus]]
[[Category: thermus thermophilus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:30:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:33 2008''

Revision as of 15:02, 21 February 2008

Image:2dtv.jpg

2dtv, resolution 2.26Å

Drag the structure with the mouse to rotate

Crystal structure of LysN, alpha-aminoadipate aminotransferase, 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

2DTV is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Active as 2-aminoadipate transaminase, with EC number 2.6.1.39 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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