Purified β-1,4-N-acetylmuramoylhydrolase (muramidase-1; EC 188.8.131.52) 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 language||English (US)|
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|Publication status||Published - Jan 1 1988|
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