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- W2336374124 abstract "A novel enzyme, which was named Nα-benzyloxycarbonyl amino acid urethane hydrolase, was purified from a cell-free extract of Streptococcus faecalis R ATCC 8043, using Nα-benzyloxycarbonyl glycine as substrate. The enzyme was purified 1300-fold with an activity yield of 8%. The purified enzyme was homogeneous by disc electrophoresis. The molecular weight of the native enzyme is about 220,000 by gel filtration, and a molecular weight of 32,000 was determined for the reduced and denatured enzyme by gel electrophoresis in sodium dodecyl sulfate. The isoelectric point was 4.48. The enzyme was inhibited by p-chloromercuribenzoate. The presence of divalent cations (i.e., Co2+ or Zn2+) is essential for its activity." @default.
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- W2336374124 date "1985-04-01" @default.
- W2336374124 modified "2023-09-27" @default.
- W2336374124 title "Isolation and Characterization of a Novel Enzyme,Nα-Benzyloxycarbonyl Amino Acid Urethane Hydrolase, fromStreptococcus faecalisR ATCC 8043" @default.
- W2336374124 doi "https://doi.org/10.1080/00021369.1985.10866837" @default.
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