Skip to main content
ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Commodity Utilization Research » Research » Publications at this Location » Publication #94318
Title: IDENTIFICATION OA A HISTIDINE ACID PHOSPHATASE (PHYA) LIKE GENE IN ARABIDOPSIS THALIANA

Author
item Mullaney, Edward
item Ullah, Abul

Submitted to: Biochemical and Biophysical Research Communications
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 8/31/1998
Publication Date: N/A
Citation: N/A

Interpretive Summary: One of the goals of agricultural science has been to obtain the complete DNA code for various plants. Having all this information would potentially contribute to the development of improved plants for agriculture. One plant that has been selected, because of it small genome size, is Arabidopsis thalina. As a result of this project we have been able to tentatively identify the product encoded by one of its genes as a histidine acid phosphatase. This is the first sequence-based evidence for this type of enzyme in a dicot plant. One important member of this class of enzyme, phytase, has recently come into prominence as a feed additive to lower phosphorus in animal manure and thus protect our environment. The primary beneficiary of this research is the animal feed industry.

Technical Abstract: A close examination of the protein sequence encoded by the Arabidopsis thaliana gene F21M12.26 reveals the gene product to be a phosphomonoesterase, acid optimum (EC 3.1.3.2). A subclass of this broad acid phosphatase is also known as 'histidine acid phosphatase.' This is the first sequence-based evidence for a 'histidine acid phosphatase' in a dicotyledon. One important member of this class of enzymes is Aspergillus niger (ficuum) phytase, which came into prominence for its commercial application as a feed additive. The putative protein from A. thaliana gene F21M12.26 shares many important features of Aspergillus phytase, namely, size, active-site sequence, catalytic dipeptide and ten cysteine residues located in the key areas of the molecule, but lacks all nine N-glycosylation sites.