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- W2233867750 abstract "This chapter elaborates the structural chemistry and the biological aspects of D-Aminopeptidase DppA. The DppA D-aminopeptidase of Bacillus subtilis 168 was discovered by screening different strains of Bacilli for their ability to hydrolyze D-alanyl-p-nitroanilide (DAla-NHPhNO2). The best production was obtained after cell lysis of aging cultures grown in an optimized medium. The determination of the N-terminal sequence of the purified enzyme identified it as the product of the dppA gene (previously named dciAA), the first ORF of the dipeptide permease (dpp) operon expressed early during sporulation. The crystal structure of B. subtilis DppA reveals an elaborate quaternary organization. The general architecture of the enzyme complex is similar to that found in ‘self-compartmentalizing’ proteases, such as the proteasomes and ClpP endopeptidase complexes. Monomeric B. subtilis DppA (274 amino acid residues) consists of two separate domains. The N-terminal domain (residues 1–119 and 132–213) is largely responsible for the construction of the active site. The DppA D-aminopeptidase of B. subtilis shares 76% identity with the product encoded by the dppA gene of B. methanolicus." @default.
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- W2233867750 date "2004-01-01" @default.
- W2233867750 modified "2023-09-25" @default.
- W2233867750 title "d-Aminopeptidase DppA" @default.
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- W2233867750 doi "https://doi.org/10.1016/b978-0-12-079611-3.50309-8" @default.
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