Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a promising antimicrobial target | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
wild-type and Y268A mutant enzymes, hanging drop vapor diffusion method, 0.002 ml of 8.0 mg/ml protein in 20 mM Tris, 5 mM DTT, and 5 mM tris(2-carboxyethyl)phosphine, pH 7.8, are mixed with 0.002 ml of precipitant solution containing 0.2 M sodium iodide, 18% w/v PEG 3350, 0.1 M Bis-Tris propane, pH 6.5, 5 mM diaminoheptanedioate, 20°C, cryoprotectant is glycerol 20% v/v, X-ray diffraction structure determination and analysis at 2.0-2.05 A resolution | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
Y268A | site-directed mutagenesis, the monomeric mutant is catalytically inactive | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
31031 | - |
2 * 31031, recombinant enzyme, mass spectrometry | Escherichia coli |
61300 | - |
recombinant enzyme, analytical ultracentrifugation | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
LL-2,6-Diaminoheptanedioate | Escherichia coli | - |
meso-Diaminoheptanedioate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene dapF | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
LL-2,6-Diaminoheptanedioate | - |
Escherichia coli | meso-Diaminoheptanedioate | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 31031, recombinant enzyme, mass spectrometry | Escherichia coli |
More | DAP epimerase from Escherichia coli exists as a functional dimer in solution and the crystal state, dimerization of bacterial diaminopimelate epimerase is essential for catalysis. Molecular dynamics simulations indicate that the DAP epimerase monomer is inherently more flexible than the dimer, suggesting that dimerization optimizes protein dynamics to support function. The dimer-monomer dissociation constant is 22 nM. The dimerization interfaceof the epimerase occurs between the N-terminal domains of the two monomers | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
DAP epimerase | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme is independent of pyridoxal 5'-phosphate | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the pyridoxal 5'-phosphate-independent racemase family of enzymes | Escherichia coli |
metabolism | meso-diaminopimelate is a biosynthetic precursor of L-lysine in bacteria | Escherichia coli |
additional information | dimerization of bacterial diaminopimelate epimerase is essential for catalysis, the enzyme exists in an open, active conformation. The active site of the enzyme resides in a cleft between the two domains with each domain contributing one of the cysteine residues important for catalysis | Escherichia coli |
physiological function | diaminopimelate epimerase is involved in the biosynthesis of meso-DAP and lysine, which are important precursors for the synthesis of peptidoglycan, housekeeping proteins, and virulence factors in bacteria | Escherichia coli |