NDLI: The isopenicillin-N acyltransferase of Penicillium chrysogenum has isopenicillin-N amidohydrolase, 6-aminopenicillanic acid acyltransferase and penicillin amidase activities, all of which are encoded by the single penDE gene

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The isopenicillin-N acyltransferase of Penicillium chrysogenum has isopenicillin-N amidohydrolase, 6-aminopenicillanic acid acyltransferase and penicillin amidase activities, all of which are encoded by the single penDE gene

Content Provider	Scilit
Author	Alvarez, Emilio Meesschaert, Boudewijn Gutierrez, Santiago Diez, Bruno Barredo, Jose L. Martin, Juan F.
Copyright Year	1993
Description	Journal: Journal of Biological Inorganic Chemistry The isopenicillin-N acyltransferase of Penicillium chrysogenum catalyzes the conversion of the biosynthetic intermediate isopenicillin N to the hydrophobic penicillins. The isopenicillin-N acyltransferase copurified with the acyl-CoA:6-aminopenicillanic acid (6-APA) acyltransferase activity which transfers an acyl residue from acyl-CoA derivatives (e.g. phenylacetyl-CoA, phenoxyacetyl-CoA) to 6-APA. Other thioesters of phenylacetic acid were also used as substrates. An amino acid sequence similar to that of the active site of thioesterases was found in the isopenicillin-N acyltransferase, suggesting that this site is involved in the transfer of phenylacetyl residues from phenylacetyl thioesters. Purified isopenicillin-N acyltransferase also showed isopenicillin-N amidohydrolase, penicillin transacylase and penicillin amidase activities. The isopenicillin-N amidohydrolase (releasing 6-APA) showed a much lower specific activity than the isopenicillin-N acyltransferase of the same enzyme preparation, suggesting that in the isopenicillin-N acyltransferase reaction the 6-APA is not released and is directly converted into benzylpenicillin. Penicillin transacylase exchanged side chains between two hydrophobic penicillin molecules; or between one penicillin molecule and 6-APA. The penicillin amidase activity is probably the reverse of the biosynthetic acyl-CoA:6-APA acyltransferase. Four P. chrysogenum mutants deficient in acyl-CoA:6-APA acyltransferase lacked the other four related activities. Transformation of these mutants with the penDE gene restored all five enzyme activities.
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1993.tb18038.x/pdf
Ending Page	332
Page Count	10
Starting Page	323
ISSN	09498257
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1993.tb18038.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	2
Volume Number	215
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1993-07-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Penicillin Amidase Activities
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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