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J. Biochem, 1995, Vol. 118, No. 3 555-561
© 1995 Japanese Biochemical Society

other

Cloning and Expression of Dipeptidase from Acinetobacter calcoaceticus ATCC 230551

Hideki Adachi2 and Masafumi Tsujimoto

Suntory Institute for Biomedical Research Shimamoto, Mishima-gun, Osaka 618

2To whom correspondence should be addressed. Tel: +81-75-962-9283, Fax: +81-75-962-6448

The gene encoding dipeptidase was cloned from Acinetobacter calcoaceticus ATCC 23055. Determination of the nucleotide sequence revealed that the gene had an open reading flame of 1, 050 bp coding a protein of 350 amino acids. The deduced amino acid sequence showed 48.8% similarity to human renal dipeptidase and conserved two amino acid residues identified in human and pig renal dipeptidases as essential ones for the catalytic activity. Purified recombinant enzyme expressed in Escherichia coli did not hydrolyze the unsaturated dipeptide, glycyldehydrophenylalanine. On the other hand, it preferentially hydrolyzed dipeptides having a D–amino acid, when compared with those having an L–ami no acid at the C–terminal. Furthermore, it could not hydrolyze tripeptides. These results indicate that the dipeptidase produced by A. calcoaceticus ATCC 23055 has a unique substrate specificity and preferentially hydrolyzes dipeptides having a D-amino acid at the C-terminal.

1The nucleotide sequence data reported in this paper will appear in the GSDB, DDBJ, EMBL, and NCBI nucleotide sequence databases with the accession number D50330 [GenBank] .


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