L. Pasamontes et al., CLONING OF THE PHYTASES FROM EMERICELLA-NIDULANS AND THE THERMOPHILICFUNGUS TALAROMYCES-THERMOPHILUS, Biochimica et biophysica acta, N. Gene structure and expression, 1353(3), 1997, pp. 217-223
Phytases (EC 3.1.3.8) belong to the family of histidine acid phosphata
ses. We have cloned the phytases of the fungi Emericella nidulans and
Talaromyces thermophilus. The putative enzyme encoded by the E. nidula
ns sequence consists of 463 amino acids and has a M-r of 51785. The pr
otein deduced from the T. thermophilus sequence consists of 466 amino
acids corresponding to a M-r of 51450. Both predicted amino acid seque
nces exhibited high identity (48% to 67%) to known phytases. This high
level of identity allowed the modelling of all available fungal phyta
ses based on the three-dimensional structure coordinates of the Asperg
illus niger phytase. By this approach we identified 21 amino acids whi
ch are conserved in fungal phyA phytases and are part of the residues
forming the substrate pocket. Furthermore, potential glycosylation sit
es were identified and compared between the aforementioned phytases an
d the A. niger phytase. (C) 1997 Elsevier Science B.V.