Document Detail


Glutamine degradation through the omega-amidase pathway in Saccharomyces cerevisiae.
MedLine Citation:
PMID:  3309146     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A glutamine transaminase activity has been identified in Saccharomyces cerevisiae, and the existence of the omega-amidase activity previously described in this yeast has been confirmed. The glutamine transaminase utilizes different 2-oxo acids as substrates, including pyruvate and glyoxylate, and is regulated by the available nitrogen source. The glutamine transaminase activity decreases when lysine or glycine is added to the medium; the inhibition by lysine diminishes under microaerophilic culture conditions.
Authors:
M Soberón; A González
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of general microbiology     Volume:  133     ISSN:  0022-1287     ISO Abbreviation:  J. Gen. Microbiol.     Publication Date:  1987 Jan 
Date Detail:
Created Date:  1987-11-09     Completed Date:  1987-11-09     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0375371     Medline TA:  J Gen Microbiol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  9-14     Citation Subset:  IM    
Affiliation:
Centro de Investigación sobre Fijación de Nitrógeno, UNAM, Cuernavaca, Morelos.
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MeSH Terms
Descriptor/Qualifier:
Amidohydrolases / metabolism*
Glutamine / metabolism*
Mutation
Phenotype
Saccharomyces cerevisiae / enzymology*,  genetics
Transaminases / metabolism
Chemical
Reg. No./Substance:
56-85-9/Glutamine; EC 2.6.1.-/Transaminases; EC 2.6.1.15/glutamine-pyruvate aminotransferase; EC 3.5.-/Amidohydrolases; EC 3.5.1.3/omega-amidase

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


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