Document Detail


Regulatory properties of an inducible aliphatic amidase in a thermophilic bacillus.
MedLine Citation:
PMID:  932686     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A thermophilic bacillus growing on acetamide as both carbon and nitrogen sources produces an inducible amidase. This amidase hydrolysed the following amides in decreasing order or activity, in comparison with acetamide (1.00): propionamide (0.97), fluoroacetamide (0.84), formamide (0.35) and glycinamide (0.12). Cyanoacetamide, dimethylacetamide, dimethylformamide and urea also induced the synthesis of the amidase, but were not substrates of the enzyme. Studies with protoplasts suggest that the amidase is located in the cytoplasm. Glucose strongly inhibited amidase synthesis; and limiting nitrogen did not release this inhibition. Urea strongly inhibited amidase activity in a competitive manner; but the inhibition caused by iodoacetamide and cyanoacetamide was non-competitive. Both thioacetamide and thiourea were effective inhibitors of enzyme induction. Bacteria grown on a succinate-minimal medium exhibited a lag in amidase synthesis, which could be eliminated by decreasing the concentration of succinate. Acetate- or pyruvate-grown cultures behaved similarly, while those grown on alanine or glutamate exhibited no lag in enzyme induction. In the mutant strain E21, repression of amidase synthesis by glucose was much less evident and no lag for induction was apparent with any of the other carbon sources mentioned.
Authors:
B Thalenfeld; N Grossowicz
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of general microbiology     Volume:  94     ISSN:  0022-1287     ISO Abbreviation:  J. Gen. Microbiol.     Publication Date:  1976 May 
Date Detail:
Created Date:  1976-08-23     Completed Date:  1976-08-23     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0375371     Medline TA:  J Gen Microbiol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  131-41     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acetamides / metabolism
Amides / metabolism
Amidohydrolases / biosynthesis*,  metabolism
Bacillus / enzymology*,  growth & development,  metabolism
Cell-Free System
Cytoplasm / enzymology
Enzyme Induction / drug effects
Enzyme Repression
Glucose / pharmacology
Hot Temperature
Kinetics
Protoplasts / enzymology
Thioacetamide / pharmacology
Thiourea / pharmacology
Urea / pharmacology
Chemical
Reg. No./Substance:
0/Acetamides; 0/Amides; 50-99-7/Glucose; 57-13-6/Urea; 62-55-5/Thioacetamide; 62-56-6/Thiourea; EC 3.5.-/Amidohydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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