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Keywords :
Bacillus subtilis 168; d-alanyl-p-nitroanilide (d-Ala-pNa); D-Aminopeptidase DppA; Active site; Amino peptidase; Bacillus subtili 168; Bacillus Subtilis; D-alanyl-p-nitroanilide; d-Amino acids; D-aminopeptidase dppa; N terminus; p-Nitroanilide; Zinc metallopeptidase; Biochemistry, Genetics and Molecular Biology (all)
Abstract :
[en] The subject of this chapter is d-aminopeptidase DppA. DppA is a cocatalytic zinc metallopeptidase that releases a d-amino acid from the N-terminus of a peptide. It has been characterized as Bacillus subtilis. The aminopeptidase is a compartmentalizing enzyme and forms a homodecamer arranged in a barrel-shape, with two rings of five monomers stacked with the ten active sites pointing towards the large, central cavity. Biologically, the enzyme degrades the d-Ala-d-Ala dipeptide derived from the cell wall cross-linking peptide, and the gene is expressed early in sporulation.
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