Author
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Mullaney, Edward |
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Daly, Catherine |
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Submitted to: Mycological Society of America
Publication Type: Proceedings Publication Acceptance Date: 5/1/2003 Publication Date: 7/27/2003 Citation: Mullaney, E.J., Daly, C.B. 2003. Conserved structural features of a putative histidine acid phosphatase encoded by a neurospora crassa gene. In: Proceedings of the Joint meeting of the Mycological Society of America and the British Mycological Society annual meeting, July 27-31, 2003, Monterey, CA. p. 75. Interpretive Summary: Technical Abstract: Several fungal phytases have been identified as being histidine acid phosphatases (HAP). This group of enzymes has a conserved amino acid sequence, RHGXRXP, previously identified as its catalytic active site. A hypothetical protein identified from the Neurospora crassa sequencing project, Locus NCU06351.1,has this characteristic active site motif, plus several other structural components that suggest that this protein is analogous to Aspergillus niger phytase. A. niger phytase, a HAP, is commercially marketed as an animal feed additive and has been extensively studied. All the principal components of both the active site and the substrate specificity site are present in this Neurospora protein. Further analysis of the DNA sequence of NCU06351.1 suggests both a different 5' end and the presence of an intron. These findings increase the similarity between this N. crassa and the A. niger phytase gene. It also appears that all the cysteine residues necessary for the five disulfide bridges in A. niger phytase are present in NCU06351.1. Isolation and characterization of this N. crassa enzyme will refine our understanding of other structurally important features of the phytase molecule. |
