ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Alkaline d-peptidase (Adp) from Bacillus cereus DF4-B is a d-stereospecific endopeptidase acting on oligopeptides composed of d-phenylalanine and the primary structure deduced from its gene, adp, shows a similarity with d-stereospecific hydrolases from Ochrobactrum anthropi strains. We have isolated DNA fragments covering the flanking region of adp from DF4-B genome and found an additional gene, adp2, located upstream of adp. The deduced amino acid sequence of Adp2 showed 96% and 85% identity with those of Adp from B. cereus strains AH559 and DF4-B, respectively. The recombinant Adp2 expressed in Escherichia coli was purified to homogeneity and characterized. It had hydrolyzing activity toward (d-Phe)3, (d-Phe)4, and (d-Phe)6 but did not act on (l-Phe)4, d-Phe-NH2, and l-Phe-NH2, some characteristics that are closely related to those of Adp from strain DF4-B. These results indicate that highly homologous genes encoding d-stereospecific endopeptidases are arranged in a tandem manner on the genomic DNA of B. cereus DF4-B.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1016/S0378-1097(03)00665-7
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