25mn | pdb_000025mn

Lysine racemase TM1597

spinqualitylabelsall models 25mn, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 25mn is a 6 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: LLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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