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• W2096004313 abstract "ABSTRACT Streptococcus milleri NMSCC 061 was screened for antimicrobial substances and shown to produce a bacteriolytic cell wall hydrolase, termed millericin B. The enzyme was purified to homogeneity by a four-step purification procedure that consisted of ammonium sulfate precipitation followed by gel filtration, ultrafiltration, and ion-exchange chromatography. The yield following ion-exchange chromatography was 6.4%, with a greater-than-2,000-fold increase in specific activity. The molecular weight of the enzyme was 28,924 as determined by electrospray mass spectrometry. The amino acid sequences of both the N terminus of the enzyme (NH 2 SENDFSLAMVSN) and an internal fragment which was generated by cyanogen bromide cleavage (NH 2 SIQTNAPWGL) were determined by automated Edman degradation. Millericin B displayed a broad spectrum of activity against gram-positive bacteria but was not active against Bacillus subtilis W23 or Escherichia coli ATCC 486 or against the producer strain itself. N -Dinitrophenyl derivatization and hydrazine hydrolysis of free amino and free carboxyl groups liberated from peptidoglycan digested with millericin B followed by thin-layer chromatography showed millericin B to be an endopeptidase with multiple activities. It cleaves the stem peptide at the N terminus of glutamic acid as well as the N terminus of the last residue in the interpeptide cross-link of susceptible strains." @default.
• W2096004313 created "2016-06-24" @default.
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• W2096004313 date "2000-01-01" @default.
• W2096004313 modified "2023-10-14" @default.
• W2096004313 title "Purification and Partial Characterization of a Murein Hydrolase, Millericin B, Produced by <i>Streptococcus milleri</i> NMSCC 061" @default.
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• W2096004313 doi "https://doi.org/10.1128/aem.66.1.23-28.2000" @default.
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