In vitro synthesis of hydrophobic penicillinase in extracts of Bacillus licheniformis,749C
Biochemical and Biophysical Research CommunicationsPublished 1 October 1975
Brian N. Dancer, J. O. Lampen
Citations16
SJR quartileQ2
SJR score0.75
SNIP0.56
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Abstract
Extracts of Bacillus licheniformis 749/C in an in vitro protein synthesis system produced the hydrophobic penicillinase containing covalently-bound phospholipid. The hydrophilic penicillinase (exoenzyme) and the hydrophobic enzyme without the phospholipid were scarcely detectable.
Keywords
Immunology and MicrobiologyMedicineBiochemistry, Genetics and Molecular Biology
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A system of transformation in Bacillus licheniformis is described, in which a wide variety of markers can be transferred from one strain to another and the electrophoretic properties of the penicillinases produced by the progeny of inter-strain crosses appeared to be affected by the type of cell in which the relevant structural gene was expressed.
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Using the escape into the medium of a normally intracellular, maltose-inducible α-glucosidase as a more sensitive indicator of cell damage than direct measurement of lysis, it was concluded that at least 40 % of the penicillinase is liberated from the cells without gross disorganization of their structure.
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At substrate concentrations (benzylpenicillin) of about one-fifth the K(m) value, whole cells show a slight permeability restriction, although this does not occur in isolated particles and protoplasts.
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The cell-bound penicillin enzyme of Bacillus licheniformis strain 749/c was examined since this material appears to be an intermediate in the formation of the exopenicillinase.
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The plasma membrane-bound penicillinase of Bacillus licheniformis 749 C has been purified and trypsin readily cleaved the glycerol-containing moiety from the enzyme protein, forming enzyme with molecular weight and heat stability like that of the exoenzyme.
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6 Citations1969Julian Davies
A cell-free protein-synthesising system from Bacillus licheniformis 749C was developed and characterised, and an attempt was made to investigate the nature of the products synthesised in vitro, suggesting a large proportion of the activity is accounted for by addition of amino acids to nascent polypeptide chains.