Disease relevance of dapF

• Nucleotide sequence of the dapF gene and flanking regions from Escherichia coli K12 [1].
• Previous attempts to express the diaminopimelate epimerase gene dapF of Mycobacterium tuberculosis in Escherichia coli resulted in undetectable enzyme yields [2].
• Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase [3].

High impact information on dapF

• An open reading frame was found upstream of sss whose protein sequence showed strong identity to DapF, the diaminopimelate epimerase [4].
• The Haemophilus influenzae diaminopimelate epimerase was cloned, expressed, purified, and crystallized in the C2221 space group (a = 102.1 A, b = 115.4 A, c = 66.3 A, alpha = beta = gamma = 90 degrees) [3].
• Diaminopimelate epimerase is a representative of the PLP-independent amino acid racemases, for which no structure has yet been determined and substantial evidence exists supporting the role of two cysteine residues as the catalytic acid and base [3].
• The xerC gene is expressed as part of a multicistronic unit that includes the dapF gene and two other open reading frames [5].
• Crystal structure of E. coli yddE protein reveals a striking homology with diaminopimelate epimerase [6].

Analytical, diagnostic and therapeutic context of dapF

• Molecular cloning, characterization, and chromosomal localization of dapF, the Escherichia coli gene for diaminopimelate epimerase [7].
• When isolated sacculi were treated with Chalaropsis N-acetylmuramidase and the resulting soluble products were analyzed by high-pressure liquid chromatography, the proportion of the main peptidoglycan dimer was lower in the dapF mutant than in the parental strain [8].

References