粪肠球菌β-1,4-N-乙酰胞壁酰水解酶与5-巯基尿苷单磷酸的共价修饰
Covalent modification of the beta-1,4-N-acetylmuramoylhydrolase of Streptococcus faecium with 5-mercaptouridine monophosphate.
作者信息
Dolinger D L, Schramm V L, Shockman G D
机构信息
Department of Microbiology, Temple University School of Medicine, Philadelphia, PA 19140.
出版信息
Proc Natl Acad Sci U S A. 1988 Sep;85(18):6667-71. doi: 10.1073/pnas.85.18.6667.
Abstract
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.
摘要
已证明来自粪肠球菌ATCC 9790的纯化β-1,4-N-乙酰胞壁酰水解酶（溶菌酶-1；EC 3.2.1.17）与大约12摩尔当量的单体5-巯基尿苷单磷酸共价取代。所有12个残基都存在于该酶经蛋白水解处理的87 kDa活性形式上。分离出一个含有5-巯基尿苷、酪氨酸、丙氨酸、甘氨酸和亮氨酸的肽片段，这与核苷酸与酪氨酸的O-磷酸键一致。
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Covalent modification of the beta-1,4-N-acetylmuramoylhydrolase of Streptococcus faecium with 5-mercaptouridine monophosphate.粪肠球菌β-1,4-N-乙酰胞壁酰水解酶与5-巯基尿苷单磷酸的共价修饰
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