R. Dijkerman et al., THE ANAEROBIC FUNGUS PIROMYCES SP STRAIN E2 - NITROGEN REQUIREMENT AND ENZYMES INVOLVED IN PRIMARY NITROGEN-METABOLISM, Archives of microbiology, 166(6), 1996, pp. 399-404
The anaerobic fungus Piromyces sp. strain E2 appeared restricted in ni
trogen utilization. Growth was only supported by ammonium as source of
nitrogen. Glutamine also resulted in growth, but this was due to rele
ase of ammonia rather than to uptake and utilization of the amino acid
. The fungus was not able to grow on other amino acids, albumin, urea,
allantoin, or nitrate. Assimilation of ammonium is very likely to be
mediated by NADP-linked glutamate dehydrogenase (NADP-GDH) and glutami
ne synthetase (GS). One transaminating activity, glutamate-oxaloacetat
e transaminase (GOT), was demonstrated. Glutamate synthase (GOGAT), NA
D-dependent glutamate dehydrogenase (NAD-GDH), and the transaminating
activity glutamate-pyruvate transaminase (GPT) were not detected in ce
ll-free extracts of Piromyces sp. strain E2. Specific enzyme activitie
s of both NADP-GDH and GS increased four- to sixfold under nitrogen-li
miting conditions.