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Cysteinyl dipeptidase from Aspergillus oryzae (CdpA) was produced in Escherichia coli and purified. The enzyme showed activity specific toward cysteine-containing dipeptides, but its substrate specificity was distinct from those of other cysteinyl dipeptidases of the M20 family. It was optimally active at pH 7-8 and stable at pH 6-9 and at up to 40 °C.

Citation

Ryota Hattori, Mayumi Matsushita-Morita, Junichiro Marui, Sawaki Tada, Satoshi Suzuki, Ikuyo Furukawa, Youhei Yamagata, Hitoshi Amano, Hiroki Ishida, Michio Takeuchi, Ken-Ichi Kusumoto. Characterization of an Aspergillus oryzae cysteinyl dipeptidase expressed in Escherichia coli. Bioscience, biotechnology, and biochemistry. 2011;75(1):159-61

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PMID: 21228467

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