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Hatanaka, T. et al.

Tadashi Hatanaka, Akihiro Yamasato, Jiro Arima, Hirokazu Usuki, Yukihiro Yamamoto, Yuya Kumagai,

Extracellular Production and Characterization of Streptomyces X-prolyl Dipeptidyl Aminopeptidase.

X-prolyl dipeptidyl aminopeptidases (X-PDAPs) are useful in various food industries. In this study, we performed sequence-based screening to obtain a stable X-PDAP enzyme from thermophilic Streptomyces strains. We found three genes that encoded X-PDAP from Streptomyces thermoluteus subsp. fuscus NBRC 14270 (14270 X-PDAP), Streptomyces thermocyaneoviolaceus NBRC 14271 (14271 X-PDAP), and Streptomyces thermocoerulescens NBRC 14273, which were subsequently cloned and sequenced. The deduced amino acid sequences of these genes showed high similarity, with ~80% identity with each other. The isolated X-PDAPs and an X-PDAP from Streptomyces coelicolor were expressed in Streptomyces lividans using a hyperexpression vector: pTONA5a. Among these genes, only 14270 and 14271 X-PDAPs caused overexpression and extracellular production without artificial signal peptides. We also characterized the biochemical properties of purified 14271 X-PDAP. In addition, we found that, in peptide synthesis via an aminolysis reaction, this enzyme recognized D: -amino acid derivatives as acyl acceptors, similar to L: -amino acid derivatives.[1]

References

Extracellular Production and Characterization of Streptomyces X-prolyl Dipeptidyl Aminopeptidase. Hatanaka, T., Yamasato, A., Arima, J., Usuki, H., Yamamoto, Y., Kumagai, Y. Appl. Biochem. Biotechnol. (2011) [Pubmed]

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