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.
Keywords
ACETONE
BUFFERS
CENTRIFUGATION
CHEMISTRY
CHROMATOGRAPHY
CULTURE MEDIA
ESCHERICHIA COLI
EXPERIMENTAL LAB STUDY
FERMENTATION
HYDROGEN-ION CONCENTRATION
METABOLISM
MICROCOCCUS
PENICILLIN G
PHARMACOLOGY
PHENYLACETATES
RADIOMETRY
SULFUR ISOTOPES
MeSH Terms
Acetone
Acylation
Buffers
Centrifugation
Chemical Phenomena
Chemistry
Chromatography
Culture Media
Escherichia coli
Fermentation
Hydrogen-Ion Concentration
Metabolism
Micrococcus
Penicillanic Acid
Penicillin G
Penicillins
Pharmacology
Phenylacetates
Radiometry
Research
Sulfur Isotopes
Chemicals
Buffers
Culture Media
Penicillins
Phenylacetates
Sulfur Isotopes
penicilloic acid
Acetone
Penicillanic Acid
penilloic acid
Penicillin G
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
PRUESS D L
JOHNSON M J
References (13)
13 references, click to expand
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Distribution and substrate specificity of benzylpenicillin acylase.
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Nature. 1964 Feb 22;201:824
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PRODUCTION OF PENICILLIN ACYLASE.
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Nature. 1964 Aug 1;203:520
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PMID: 14084584
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PMID: 13587479
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PMID: 13672975
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Proc Soc Exp Biol Med. 1963 Aug-Sep;113:1008-12
PMID: 14073094
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Nature. 1964 Aug 1;203:519-20
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