Nitrogen metabolism in Aspergillus parasiticus NRRL 3240 and A. flavus NRRL 3537 in relation to aflatoxin production.
The relationship between nitrogen assimilation, metabolism and aflatoxin formation has been investigated in a toxigenic and a non-toxigenic strain of Aspergillus parasiticus. Ammonia from the medium is mainly assimilated via NADP-requiring glutamate dehydrogenase. During growth NAD-requiring glutamate dehydrogenase followed an inverse pattern of activity with respect to NADP glutamate dehydrogenase. Alpha-ketoglutarate, the product of NAD glutamate dehydrogenase, stimulated acetate incorporation into aflatoxins. Glutamine synthetase, ornithine transcarbamylase, both utilizing glutamate as substrate were assayed under different growth conditions. An important regulatory role for glutamine synthetase is suggested. The metabolic route of asparagine utilization was also investigated. Both the known pathways, glutamate oxaloacetate transaminase and glutamate pyruvate transaminase are operative simultaneously.
Bhatnagar
R K
RK
Ahmad
S
S
Mukerji
K G
KG
Venkitasubramanian
T A
TA
D000348:Aflatoxins / Q000096:biosynthesis*; D000410:Alanine Transaminase / Q000378:metabolism; D001216:Asparagine / Q000378:metabolism; D001230:Aspergillus / Q000378:metabolism*; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D009584:Nitrogen / Q000378:metabolism*; D009954:Ornithine Carbamoyltransferase / Q000378:metabolism; D013997:Time Factors; D015032:Zinc / Q000378:metabolism
D000348:Aflatoxins; D001216:Asparagine; D005969:Glutamate Dehydrogenase; D009954:Ornithine Carbamoyltransferase; D000410:Alanine Transaminase; D005974:Glutamate-Ammonia Ligase; D015032:Zinc; D009584:Nitrogen