Amino-acid substitutions in the cleavage site of acyl-coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum: effect on proenzyme cleavage and activity.

No abstract is available for this paper.

• Publication year

  1995

• Venue

  Gene

• Publication date

  1995-08-30

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/0378-1119(95)00369-HPMID 7557412
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Penicillin acylase has a single-amino-acid catalytic centre

  1996cited by this paper
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  1994cited by this paper
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  1993cited by this paper
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  1993cited by this paper
• 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.

  1993cited by this paper
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  1993cited by this paper
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  1993cited by this paper
• On the production of α,β‐heterodimeric acyl‐coenzyme A: isopenicillin N‐acyltransferase of Penicillium chrysogenum

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  1992cited by this paper
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  1992cited by this paper
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  1991cited by this paper
• Acyl-CoA: 6-APA acyltransferase from Penicillium chrysogenum studies on its hydrolytic activity.

  1991cited by this paper
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  1990cited by this paper
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  1990cited by this paper
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  1980cited by this paper
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  1977cited by this paper
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  1975cited by this paper
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