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- W2013598989 abstract "1. A 12–20-fold purification of the nisin-inactivating enzyme from Bacillus cereus has been achieved in yields of 25–40%. 2. The enzyme inactivated nisins A, B, C and E but not nising D, and it was unable to inactivate the antibiotics penicillin, erythromycin, neomycin, streptomycin and tylosin. Since the enzyme also inactivates subtilin1, the evidence suggests that the enzyme is specific for a particular group which occurs in the peptide antibiotics nisin and subtilin. 3. The Km values for nisins A, B, C and E were 33 · 10−3, 35 · 10−3, 1.74 · 10−3 and 1.26 · 10−3M, respectively. These results suggest stereochemical differences between the nisins. 4. Chemical studies of enzymically inactivated nisin showed that the C-terminal sequence of dehydroalanyllysine was reduced to alanyllysine and it is suggested, therefore, that the enzyme is a dehydropeptide reductase." @default.
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- W2013598989 date "1971-02-01" @default.
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- W2013598989 title "Partial purification, specificity and mechanism of action of the nisin-inactivating enzyme from Bacillus cereus" @default.
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- W2013598989 doi "https://doi.org/10.1016/0005-2744(71)90056-8" @default.
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