دورية أكاديمية
Primary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data
| العنوان: | Primary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data |
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| المؤلفون: | Joris, Bernard, Jacques, Philippe, Frère, Jean-Marie, Ghuysen, Jean-Marie, Van Beeumen, J. |
| المصدر: | European Journal of Biochemistry, 162 (3), 519-524 (1987) |
| بيانات النشر: | Blackwell Science, 1987. |
| سنة النشر: | 1987 |
| مصطلحات موضوعية: | amino acid sequence, amino acids/analysis, binding sites, cyanogen bromide, hydrolysis, kinetics, muramoylpentapeptide carboxypeptidase/antagonists & inhibitors/*isolation, purification, penicillanic acid, peptide fragments/isolation & purification, phthalic acids, streptomyces/*enzymology, sulfhydryl compounds/analysis, trypsin, Life sciences, Microbiology, Biochemistry, biophysics & molecular biology, Sciences du vivant, Microbiologie, Biochimie, biophysique & biologie moléculaire |
| الوصف: | In order to confirm the Streptomyces codon usage, the Streptomyces R61 DD-peptidase was fragmented by cyanogen bromide cleavage of the carboxymethylated protein, trypsin digestion of the carboxymethylated protein and trypsin digestion of the protein treated with beta-iodopenicillinate and endoxo-delta 4-tetrahydrophthalic acid. The isolated peptides, which altogether represented more than 50% of the polypeptide chain, were sequenced. The data thus obtained were in excellent agreement with the primary structure of the protein as deduced from the nucleotide sequence of the cloned gene. Though a weak acylating agent, beta-iodopenicillanate reacted selectively with the active site of the DD-peptidase and formed an adduct which mas much more stable than that formed with benzylpenicillin, thus facilitating the isolation and characterization of the active-site peptide. |
| نوع الوثيقة: | journal article http://purl.org/coar/resource_type/c_6501Test article |
| اللغة: | English |
| العلاقة: | urn:issn:0014-2956; urn:issn:1432-1033 |
| DOI: | 10.1111/j.1432-1033.1987.tb10670.x |
| الوصول الحر: | https://orbi.uliege.be/handle/2268/83564Test |
| حقوق: | open access http://purl.org/coar/access_right/c_abf2Test info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsorb.83564 |
| قاعدة البيانات: | ORBi |
| DOI: | 10.1111/j.1432-1033.1987.tb10670.x |
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