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L-histidine utilization in Aspergillus nidulans.

M A Polkinghorne, M J Hynes

Journal of Bacteriology

|March 1, 1982

Summary

Histidase activity limits histidine utilization in Aspergillus nidulans, not uptake. The fungus cannot convert histidine to L-glutamate, accumulating urocanate due to a lack of urocanase.

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Area of Science:

Biochemistry
Mycology
Metabolic Regulation

Background:

Fungi utilize various nitrogen sources for growth.
L-histidine metabolism is crucial for fungal nitrogen assimilation.
Aspergillus nidulans's specific metabolic pathways require elucidation.

Purpose of the Study:

Determine the limiting factor for histidine utilization as a sole nitrogen source in Aspergillus nidulans.
Investigate the inability of histidine to serve as a sole carbon source.
Characterize the regulation of histidase synthesis and activity.

Main Methods:

Enzyme activity assays for histidase and urocanase.
Metabolite analysis of histidine, urocanate, and glutamate.
Nitrogen metabolite repression studies.
Nitrate control investigations.

Main Results:

Histidase activity, not L-histidine uptake, limits nitrogen utilization.
Histidine is quantitatively converted to extracellular urocanate due to absent urocanase.
Histidine cannot be converted to L-glutamate in vivo.
Histidase synthesis is regulated by nitrogen metabolite repression and requires a carbon source.
Histidase activity is inhibited by urocanate, L-glutamate, and L-glutamine.

Conclusions:

Histidase activity is the primary determinant for using histidine as a nitrogen source in Aspergillus nidulans.
The absence of urocanase prevents histidine's conversion to L-glutamate, precluding its use as a carbon source.
Histidine metabolism in this fungus is subject to complex regulatory controls, including nitrogen metabolite repression and product inhibition.

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