Biosynthesis of the Peptidoglycan of Bacterial Cell Walls
Year: 1970
Type: article
Abstract: The binding of radioactive penicillin G to a particulate enzyme preparation derived from Bacillus subtilis has been examined. The binding required an intact β-lactam ring and showed saturation kinetics. About 49 µµmoles of penicillin G were bound per mg of enzyme protein. The binding was reversed by neutral hydroxylamine, ethanethiol, or H2O2. The product of reversal with hydroxylamine was identified as penicilloyl hydroxamate, and that with ethanethiol after methylation as α-ethylthio-β-methylbenzylpenicilloate. The binding was also prevented by prior reaction of the particulate enzyme preparation with sulfhydryl reagents such as iodoacetate. These data indicate that penicillin G reacted with some component of the particulate enzyme preparation to form a thiol ester of penicilloic acid and a functional thiol group in the enzyme preparation.
Source: Journal of Biological Chemistry
Authors: Paul J. Lawrence, Jack L. Strominger
Institutions: Harvard University, University of Utah
Language: English
Subfield: Genetics
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W3119994227