EC Number   |
General Information |
Reference |
|---|
    2.6.1.83 | malfunction |
Arabidopsis thaliana DAP mutant dapat shows reduced activity of the Lys biosynthesis enzyme L,L-diaminopimelate aminotransferase, physiological and metabolic impacts of impaired Lys biosynthesis, the mutation leads to metabolic shifts and growth inhibition, phenotype, overview. No differences in dark respiration between genotypes are observed, but a lower storage and consumption of starch and sugars is observed in dapat plants, also higher protein turnover but no differences in total amino acids during a diurnal cycle in dapat plants. Biochemical alterations rather than stomatal limitations are responsible for the decreased photosynthesis and growth of the dapat mutant, which mimics stress conditions associated with impairments in the Lys biosynthesis pathway |
-, 759568 |
| 2.6.1.83 | metabolism |
the enzyme is involved in the lysine pathway, overview. Lysine is synthetized in the chloroplast using aspartate as a precursor. Dihydrodipicolinate synthase (DHDPS) is the first enzyme of lysine biosynthesis and it requires pyruvate export from the cytosol to the chloroplast. Under stress conditions, lysine is exported from the chloroplast to mitochondria to be degraded, and electrons are used as a donor for ATP synthesis |
-, 759568 |
| 2.6.1.83 | metabolism |
the LL-diaminopimelate aminotransferase (DapL) pathway is a variant of the lysine biosynthetic pathway, overview |
759252 |
| 2.6.1.83 | more |
comparative molecular dynamics simulations, ligand docking study, sequence comaprisons and three-dimensional homology modelling, active site structure, detailed overview. Key conserved active site residues are identified as I43, G44, Y74, E77, K111, Y134, N189, K251, N294, and R390 |
759252 |
| 2.6.1.83 | more |
DapL enzyme structures comparisons |
758829 |
| 2.6.1.83 | physiological function |
DapL is a homodimer that catalyzes the conversion of tetrahydrodipicolinate to LL-diaminopimelate in a single transamination reaction. The penultimate and ultimate products of the lysine biosynthesis pathway, meso-diaminopimelate and lysine, are key components of the Gram-negative and Gram-positive bacterial peptidoglycan cell wall |
759252 |
| 2.6.1.83 | physiological function |
lysine biosynthesis pathway |
725250 |
| 2.6.1.83 | physiological function |
the Verrucomicrobium spinosum dapL gene encodes a putative diaminopimelate aminotransferase, the gene expression rescues an Escherichia coli strain that is auxotrophic for meso-diaminopimelate. LL-Diaminopimelate aminotransferase is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the transamination of L-tetrahydrodipicolinate to form LL-diaminopimelate. The reaction proceeds via a bimolecular ping-pong mechanism. First, the amino group from the donor molecule L-glutamate forms a covalent Schiff base with the PLP molecule tethered in the enzyme active site. This is followed by the transfer of the amino group to the acceptor molecule, L-tetrahydrodipicolinate, forming LL-diaminopimelate. Subsequent enzymes catalyze the epimerization to form meso-diaminopimelate and decarboxylation to yield L-lysine |
758829 |
