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  Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium

Neugebauer, K., Sprengel, R., & Schaller, H. (1981). Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium. Nucleic Acids Research, 9(11), 2577-2588. doi:10.1093/nar/9.11.2577.

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NuclAcidRes_9_1981_2577.pdf (Any fulltext), 556KB
 
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 Creators:
Neugebauer, Kristina, Author
Sprengel, Rolf1, 2, 3, Author           
Schaller, Heinz, Author
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1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Rolf Sprengel Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497741              
3Olfaction Web, Max Planck Institute for Medical Research, Max Planck Society, ou_1497733              

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Free keywords: DNA, amino acids
 Abstract: The gene for the penicillinase from B. licheniformis has been cloned in a functional stat on a 1.5 kb DNA fragment and its nucleotide sequence has been determined. A sequence of 307 amino acid residues is infered for the penicillinase precursor. Of these 34 amino acids precede the sequence of the secreted form of the enzyme. This peptide extension shows the features of a signal for secretion and also provides the hydrophobic anchor for the membrane-bound form of the enzyme.

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Language(s): eng - English
 Dates: 1981-04-3019811981-06-01
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Nucleic Acids Research
  Other : Nucleic Acids Res.
Source Genre: Journal
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Pages: - Volume / Issue: 9 (11) Sequence Number: - Start / End Page: 2577 - 2588 Identifier: ISSN: 0301-5610
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000262810