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PMID: 2145504 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Glutamine metabolism and cycling in Neurospora crassa.

Microbiological reviews ·Vol. 54 ·No. 3 ·1990-09-00 ·Pages 293-304

Mora J

Abstract

Evidence for the existence of a glutamine cycle in Neurospora crassa is reviewed. Through this cycle glutamine is converted into glutamate by glutamate synthase and catabolized by the glutamine transaminase-omega-amidase pathway, the products of which (2-oxoglutarate and ammonium) are the substrates for glutamate dehydrogenase-NADPH, which synthesizes glutamate. In the final step ammonium is assimilated into glutamine by the action of a glutamine synthetase (GS), which is formed by two distinct polypeptides, one catalytically very active (GS beta), and the other (GS alpha) less active but endowed with the capacity to modulate the activity of GS alpha. Glutamate synthase uses the amide nitrogen of glutamine to synthesize glutamate; glutamate dehydrogenase uses ammonium, and both are required to maintain the level of glutamate. The energy expended in the synthesis of glutamine drives the cycle. The glutamine cycle is not futile, because it is necessary to drive an effective carbon flow to support growth; in addition, it facilitates the allocation of nitrogen or carbon according to cellular demands. The glutamine cycle which dissipates energy links catabolism and anabolism and, in doing so, buffers variations in the nutrient supply and drives energy generation and carbon flow for optimal cell function.

MeSH Terms
Glutamine/metabolism Neurospora crassa/metabolism
Chemicals
Glutamine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Mora J
Centro de Investigación Sobre Fijación de Nitrógeno, Universidad Nacional Autónoma de México, Cuernavaca, Morelos.
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Article Info
Journal
Microbiological reviews
Abbr.
Microbiol Rev
ISSN
0146-0749
DOI
10.1128/mr.54.3.293-304.1990
Published
1990-09-00
Pages
293-304
Language
English
Region
United States
NLM ID
7806086
PMCID
PMC372778
Subset
IM
External Links
PubMed source DOI: 10.1128/mr.54.3.293-304.1990 PMC Full Text
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