The Journal of Antibiotics
Online ISSN : 1881-1469
Print ISSN : 0021-8820
ISSN-L : 0021-8820
SUBSTRATE SPECIFICITY OF PENICILLIN ACYLASE OF E. COLI
ANNEMIE PLASKIEEUGENE ROETSHUBERT VANDERHAEGHE
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1978 年 31 巻 8 号 p. 783-788

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The hydrolysis of several phenylacetylamino compounds was studied using a purified preparation of E. coli penicillin acylase. The L-isomers of phenylacetyl amino acids were cleaved much faster than the D-isomers. The same observation was made for some phenylacetylamino β-lactams. When the β-lactam ring is incorporated in a penam or cephem ring system, the D-isomers were hydrolysed somewhat faster than the L-isomers. We also confirmed that benzylpenicillins with an hydroxy- or an amino-group in α-position of the side chain were hydrolysed, both in the normal and the 6-epi-series.
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© Japan Antibiotics Research Association
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