Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aspergillus oryzae / enzymology*
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Cloning, Molecular
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Cysteine / metabolism*
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Dipeptidases / biosynthesis
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Dipeptidases / genetics*
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Dipeptidases / isolation & purification
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Dipeptidases / metabolism*
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Escherichia coli / genetics*
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Gene Expression
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Humans
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Oligopeptides / metabolism
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Substrate Specificity
Substances
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Oligopeptides
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Dipeptidases
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dipeptidase
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Cysteine