Proline-Specific Extracellular Aminopeptidase Purified from <Emphasis Type="Italic">Streptomyces lavendulae</Emphasis> |
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Authors: | Arya Nandan Ashok Pandey Kesavan Madhavan Nampoothiri |
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Institution: | (1) Biotechnology Division, National Institute for Interdisciplinary Science and Technology (NIIST), CSIR, Trivandrum, Thiruvananthapuram, 695 019, Kerala, India; |
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Abstract: | Aminopeptidases catalyze the cleavage of specific amino acids from the amino terminus of protein or peptide substrates. A
proline-specific aminopeptidase was purified to homogeneity from the culture-free extract of Streptomyces lavendulae ATCC 14162 in sequential steps comprising ammonium sulfate precipitation, ultra-filtration, and column chromatography on
Q-sepharose and Sephadex G-100. The purified protein showed approximately 60 kDa in SDS-PAGE and was optimally active at pH
6.5 and 40 °C. Kinetic studies showed a K
m and V
max of 0.23 mM and 0.087 μmol/min, respectively, using Pro-p-NA, the substrate with maximum specificity. Enzyme activity was inhibited by PMSF and ions like Zn2+, Co2+, and Ni2+. However, unlike other aminopeptidases, the activity was enhanced in the presence of DTT, 1,10-phenanthroline, EDTA, amastatin,
and bestatin. Ions like Ca2+, Mg2+, and Mn2+ also enhanced the activity. |
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Keywords: | |
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