7VID
The crystal structure of L-leucine dehydrogenase from Pseudomonas aeruginosa
Summary for 7VID
| Entry DOI | 10.2210/pdb7vid/pdb |
| Descriptor | Leucine dehydrogenase, GLYCEROL (3 entities in total) |
| Functional Keywords | pseudomonas aeruginosa, pa3418, leucine dehydrogenase, branched chain amino acid, oxidoreductase |
| Biological source | Pseudomonas aeruginosa PAO1 |
| Total number of polymer chains | 2 |
| Total formula weight | 73184.79 |
| Authors | Kim, S.,Kang, W.,Yang, J.K. (deposition date: 2021-09-26, release date: 2022-06-29, Last modification date: 2023-11-29) |
| Primary citation | Kim, S.,Koh, S.,Kang, W.,Yang, J.K. The Crystal Structure of L-Leucine Dehydrogenase from Pseudomonas aeruginosa. Mol.Cells, 45:495-501, 2022 Cited by PubMed Abstract: Leucine dehydrogenase (LDH, EC 1.4.1.9) catalyzes the reversible deamination of branched-chain L-amino acids to their corresponding keto acids using NAD as a cofactor. LDH generally adopts an octameric structure with symmetry, generating a molecular mass of approximately 400 kDa. Here, the crystal structure of the LDH from (-LDH) was determined at 2.5 Å resolution. Interestingly, the crystal structure shows that the enzyme exists as a dimer with symmetry in a crystal lattice. The dimeric structure was also observed in solution using multiangle light scattering coupled with size-exclusion chromatography. The enzyme assay revealed that the specific activity was maximal at 60°C and pH 8.5. The kinetic parameters for three different amino acid and the cofactor (NAD) were determined. The crystal structure represents that the subunit has more compact structure than homologs' structure. In addition, the crystal structure along with sequence alignments indicates a set of non-conserved arginine residues which are important in stability. Subsequent mutation analysis for those residues revealed that the enzyme activity reduced to one third of the wild type. These results provide structural and biochemical insights for its future studies on its application for industrial purposes. PubMed: 35698914DOI: 10.14348/molcells.2022.0012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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