| Formation of some extracellular enzymes during the exponential growth of Bacillus subtilis. | |
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MedLine Citation:
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PMID: 3131218 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The formation of the exoenzymes, neutral and alkaline proteinase as well as alpha-amylase of Bacillus subtilis, is characterized by the same time course. The exoenzyme formation starts in the exponential phase of growth by an excess of C and N sources. We assume that carbon metabolism of pyruvate is responsible for the exoenzyme formation during this growth phase. The proteinase formation at the transient and/or stationary phase of growth is related to amino acid limitation. |
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Authors:
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P Liebs; K Riedel; J P Graba; D Schrapel; U Tischler |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Folia microbiologica Volume: 33 ISSN: 0015-5632 ISO Abbreviation: Folia Microbiol. (Praha) Publication Date: 1988 |
Date Detail:
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Created Date: 1988-07-14 Completed Date: 1988-07-14 Revised Date: 2012-07-10 |
Medline Journal Info:
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Nlm Unique ID: 0376757 Medline TA: Folia Microbiol (Praha) Country: CZECHOSLOVAKIA |
Other Details:
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Languages: eng Pagination: 88-95 Citation Subset: IM |
Affiliation:
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Central Institute of Molecular Biology, GDR, Berlin. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Alanine
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metabolism Bacillus subtilis / enzymology, growth & development*, metabolism Endopeptidases / biosynthesis Extracellular Space / enzymology*, microbiology Kinetics Metalloendopeptidases / biosynthesis Pyruvates / metabolism Pyruvic Acid Serine Endopeptidases* alpha-Amylases / biosynthesis |
| Chemical | |
Reg. No./Substance:
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0/Pyruvates; 127-17-3/Pyruvic Acid; 56-41-7/Alanine; EC 3.2.1.1/alpha-Amylases; EC 3.4.-/Endopeptidases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.62/microbial serine proteinases; EC 3.4.24.-/Metalloendopeptidases; EC 3.4.24.-/neutral proteinase, cervical |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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