Covalent modification of the β-1,4-N-acetylmuramoylhydrolase of Streptococcus faecium with 5-mercaptouridine monophosphate

D. L. Dolinger, V. L. Schramm, G. D. Shockman

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Purified β-1,4-N-acetylmuramoylhydrolase (muramidase-1; EC of Streptococcus faecium ATCC 9790 has been shown to be covalently substituted with ≃12 mol equivalents of monomeric 5-mercaptouridine monophosphate. All 12 residues are present on the proteolytically processed 87-kDa active form of the enzyme. A peptide fragment containing 5-mercaptouridine, tyrosine, alanine, glycine, and leucine was isolated consistent with an O-phosphate linkage of the nucleotide to tyrosine.

Original languageEnglish (US)
Pages (from-to)6667-6671
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number18
Publication statusPublished - Jan 1 1988
Externally publishedYes


ASJC Scopus subject areas

  • General

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