View source for 25mn


==Lysine racemase TM1597==
<StructureSection load='25mn' size='340' side='right'caption='[[25mn]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[25mn]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=25MN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=25MN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=25mn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=25mn OCA], [https://pdbe.org/25mn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=25mn RCSB], [https://www.ebi.ac.uk/pdbsum/25mn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=25mn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSRA_THEMA LYSRA_THEMA] Catalyzes the interconversion of D-lysine and L-lysine. Has also high activity toward ornithine, and weaker activity toward alanine. Contributes to production of D-lysine and D-alanine for use as peptidoglycan components.<ref>PMID:30548096</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The hyperthermophilic bacterium Thermotoga maritima contains a peptidoglycan comprising d-alanine, d-glutamate, and d-lysine. We have previously identified the biosynthetic pathways of d-lysine and d-glutamate; however, the biosynthetic pathway of d-alanine is unclear in T. maritima. The present study elucidated the d-alanine biosynthetic pathway in T. maritima, following the characterization of the TTHA0062 activity, constructed a TTHA0062 (encoding alanine racemase)-deficient Thermus thermophilus (DeltaTTHA0062) strain. TTHA0062 exhibited the racemase activity toward 10 amino acids including Ala, and the catalytic efficiency of l-alanine was twofold higher than that of d-alanine. Regarding the T. maritima genes introduced into the genome of the DeltaTTHA0062 strain, TM1597 (lysine racemase) completely restored the growth, TM1270 (multifunctional enzyme) resulted in partial restoration, whereas TM0831 (d-amino acid aminotransferase) had no effect, suggesting that TM1597 and TM1270 are involved in d-alanine biosynthesis in T. maritima. Furthermore, we determined the crystal structure of TM1597 in the internal aldimine form, in which pyridoxal 5'-phosphate (PLP) forms a Schiff base linkage with the active site residue Lys36, and revealed the residues crucial for the catalytic reaction by TM1597 mutational analysis.

Elucidation of d-alanine biosynthetic pathways in the hyperthermophiles: Characterization of alanine racemase from Thermus thermophilus and the structure and dual physiological functions of lysine racemase from Thermotoga maritima.,Miyamoto T, Moriya T, Nitta S, Fushinobu S Arch Biochem Biophys. 2026 Sep 21;786:111010. doi: 10.1016/j.abb.2026.111010. PMID:42767480<ref>PMID:42767480</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 25mn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Fushinobu S]]
[[Category: Miyamoto T]]
[[Category: Nitta S]]