Affiliation:
1. Department of Biochemistry, University of Wisconsin, Madison, Wisconsin
Abstract
Pruess, David
L. (University of Wisconsin, Madison),
and Marvin J. Johnson
. Enzymatic deacylation of S
35
-benzylpenicillin. J. Bacteriol.
90:
380–383. 1965.—S
35
-benzylpenicillin, penicilloic acid, and penilloic acid were deacylated by cell suspensions of
Escherichia coli
and
Micrococcus roseus
. Both cultures deacylated penicillin most rapidly and penilloic acid least rapidly. The deacylase activity of
M. roseus
against penicilloic acid was cell-bound, probably requiring a metal ion for activity.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
35 articles.
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