The Catalytic Activity and Penicillin Sensitivity in the Liquid and Frozen States of Membrane-Bound and Detergent-Solubilised Transpeptidase of Streptomyces R61
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1975.tb02206.x/fullpdf
Reference9 articles.
1. dd -Carboxypeptidase-Transpeptidase and Killing Site of β-Lactam Antibiotics in Streptomyces Strains R39, R61, and K11
2. Membrane-Bound Transpeptidase and Penicillin Binding Sites in Streptomyces Strain R61
3. THE PENICILLIN RECEPTOR IN STREPTOMYCES
4. Molecular weight and amino acid composition of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R61
5. Kinetics of concomitant transfer and hydrolysis reactions catalysed by the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R61
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1. Streptomyces K15 d-Ala-d-Ala Transpeptidase;Handbook of Proteolytic Enzymes;2013
2. Determination of fatty acids of the bacteria Streptomyces R61 and Actinomadura R39 by capillary gas chromatography—mass spectrometry;Journal of Chromatography B: Biomedical Sciences and Applications;1985-01
3. Penicillin-Sensitive Enzymes in Peptidoglycan Biosynthesis;CRC Critical Reviews in Microbiology;1984-01
4. Penicillin binding proteins and model transpeptidase activity of the plasma membranes ofStreptomycesstrains R61 andrimosus;FEMS Microbiology Letters;1981-11
5. Inhibition of Bacillus subtilis aminopeptidase D by β-lactam antibiotics;Biochimica et Biophysica Acta (BBA) - Enzymology;1980-12
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