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

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

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Purified β-1,4-N-acetylmuramoylhydrolase (muramidase-1; EC 3.2.1.17) 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
Volume85
Issue number18
StatePublished - 1988
Externally publishedYes

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Enterococcus faecium
Tyrosine
Peptide Fragments
Muramidase
Leucine
Alanine
Glycine
Nucleotides
Phosphates
Enzymes
5-mercaptouridylic acid
Enterococcus hirae

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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abstract = "Purified β-1,4-N-acetylmuramoylhydrolase (muramidase-1; EC 3.2.1.17) 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.",
author = "Dolinger, {D. L.} and Schramm, {Vern L.} and Shockman, {G. D.}",
year = "1988",
language = "English (US)",
volume = "85",
pages = "6667--6671",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
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T1 - Covalent modification of the β-1,4-N-acetylmuramoylhydrolase of Streptococcus faecium with 5-mercaptouridine monophosphate

AU - Dolinger, D. L.

AU - Schramm, Vern L.

AU - Shockman, G. D.

PY - 1988

Y1 - 1988

N2 - Purified β-1,4-N-acetylmuramoylhydrolase (muramidase-1; EC 3.2.1.17) 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.

AB - Purified β-1,4-N-acetylmuramoylhydrolase (muramidase-1; EC 3.2.1.17) 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.

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VL - 85

SP - 6667

EP - 6671

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

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