Reference : Primary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid s...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83564
Primary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data
English
Joris, Bernard mailto [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > >]
Jacques, Philippe mailto [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > >]
Frère, Jean-Marie mailto [Université de Liège - ULiège > Facultée de Médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > >]
Van Beeumen, J. [Rijksuniversiteit-Gent > Laboratorium voor Microbiologie > > >]
2-Feb-1987
European Journal of Biochemistry
Blackwell Science
162
3
519-524
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] 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
[en] 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.
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/83564
10.1111/j.1432-1033.1987.tb10670.x

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