Covalent modification of the beta-1,4-N-acetylmuramoylhydrolase of Streptococcus faecium with 5-mercaptouridine monophosphate.
Purified beta-1,4-N-acetylmuramoylhydrolase (muramidase-1; EC 3.2.1.17) of Streptococcus faecium ATCC 9790 has been shown to be covalently substituted with approximately 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.
Dolinger
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DL
Department of Microbiology, Temple University School of Medicine, Philadelphia, PA 19140.
Schramm
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VL
Shockman
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GD
D013058:Mass Spectrometry; D009113:Muramidase / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013291:Streptococcus / Q000201:enzymology*; D013873:Thionucleotides; D014500:Uracil Nucleotides / Q000494:pharmacology*; D014542:Uridine Monophosphate / Q000031:analogs & derivatives / Q000494:pharmacology*
D013873:Thionucleotides; D014500:Uracil Nucleotides; C035002:5-mercaptouridylic acid; D014542:Uridine Monophosphate; D009113:Muramidase