Abstract
PREVIOUS work on a cell-bound bacterial enzyme which catalyses a reversible enzymatic cleavage of benzyl penicillin to 6-aminopenicillanic acid (6-APA) and phenylacetic acid had shown that this enzyme represents an acyl transferase which, under suitable conditions, is able to synthesize penicillins by transferring acyl- and α-aminoacyl residues from acylamino acids, acyl amides, acyl-atedhydroxycarboxylic acids, mercaptocarboxylic acids, alcohols, phenols and thiophenols to the amino group of 6-APA (refs. 1–3). Free amino-acids, ammonia, hydroxy-carboxylic acids, mercaptocarboxylic acids, alcohols phenol and thiophenol, liberated in the course of these reactions, may be considered to be hydrolysis products of the acyl compounds used.
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References
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KAUFMANN, W., BAUER, K. Variety of Substrates for a Bacterial Benzyl Penicillin-splitting Enzyme. Nature 203, 520 (1964). https://doi.org/10.1038/203520a0
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DOI: https://doi.org/10.1038/203520a0
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