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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Commodity Utilization Research » Research » Publications at this Location » Publication #152590
Title: CONSERVATION OF ACTIVE SITE AND ESSENTIAL STRUCTURAL COMPONENTS ENCODED BY A PUTATIVE NEUROSPORA CRASSA PHYTASE GENE

Author
item Mullaney, Edward
item Daly, Catherine

Submitted to: Fungal Genetics Conference Proceedings
Publication Type: Proceedings
Publication Acceptance Date: 5/1/2003
Publication Date: 8/20/2003
Citation: Mullaney, E.J., Daly, C.B. 2003. Conservation of active site and essential structural components encoded by a putative neurospora crassa phytase gene. In: Proceedings of the Fungal Genetics Conference, March 18-23, 2003, Pacific Grove, CA. p. 75.

Interpretive Summary:

Technical Abstract: The Neurospora crassa sequencing project has identified many hypothetical proteins. One such protein, Locus NCU06351.1, has been reported as having the conserved sequence unique to the histidine acid phosphatase class of enzyme. Aspergillus niger phytase is a member of this class of enzyme. The gene for this enzyme has been cloned, over-expressed, and its product is now commercialized as an animal feed additive with an annual market value of over $500 million. A study of the amino acid sequence of NCU06351.1 reveals additional evidence that it is analogous to Aspergillus phytase. All the essential components of the active site and the substrate specificity site are present in this putative Neurospora protein. Remarkably, it also appears that all the constituents of the five disulfide bridges found in Aspergillus phytase have been conserved in NCU06351.1. These disulfide bridges seem to have a vital role not only in the folding pathway, but also in maintaing the proper configuration of the molecule for catalytic activity. As more is learned about the structure and function of other fungal phytases, ascribing characteristics to this putative Neurospora phytase will become more precise.