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Gene Review:

adP - alkaline D-peptidase

Bacillus cereus ATCC 10987

Asano, Y. et al., Komeda, H. et al.

Asano, Ito, Dairi, Kato,

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Disease relevance of adP

We purified a novel extracellular D-stereospecific endopeptidase, alkaline D-peptidase (D-stereospecific peptide hydrolase, EC 3.4.11.-), to homogeneity from the culture broth of the soil bacterium Bacillus cereus strain DF4-B [1].
This enzyme, DaaA, is composed of 363 amino-acid residues (molecular mass 40 082 Da), and the deduced amino-acid sequence exhibits homology to alkaline D-peptidase from Bacillus cereus DF4-B (32% identity), DD-peptidase from Streptomyces R61 (29% identity), and other penicillin-recognizing proteins [2].

High impact information on adP

The gene coding for alkaline D-peptidase (adp) was cloned into plasmid pUC118, and a 1164-base pair open reading frame consisting of 388 codons was identified as the adp gene [1].

References

An alkaline D-stereospecific endopeptidase with beta-lactamase activity from Bacillus cereus. Asano, Y., Ito, H., Dairi, T., Kato, Y. J. Biol. Chem. (1996) [Pubmed]
Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3. Komeda, H., Asano, Y. Eur. J. Biochem. (2000) [Pubmed]

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