Pasamontes L, Haiker M, Henriquez-Huecas M, Mitchell D B, van Loon A P
F. Hoffmann-La Roche Ltd., Vitamins and Fine Chemicals Division, Basel, Switzerland.
Biochim Biophys Acta. 1997 Sep 12;1353(3):217-23. doi: 10.1016/s0167-4781(97)00107-3.
Phytases (EC 3.1.3.8) belong to the family of histidine acid phosphatases. We have cloned the phytases of the fungi Emericella nidulans and Talaromyces thermophilus. The putative enzyme encoded by the E. nidulans sequence consists of 463 amino acids and has a Mr of 51785. The protein deduced from the T. thermophilus sequence consists of 466 amino acids corresponding to a Mr of 51450. Both predicted amino acid sequences exhibited high identity (48% to 67%) to known phytases. This high level of identity allowed the modelling of all available fungal phytases based on the three-dimensional structure coordinates of the Aspergillus niger phytase. By this approach we identified 21 amino acids which are conserved in fungal phyA phytases and are part of the residues forming the substrate pocket. Furthermore, potential glycosylation sites were identified and compared between the aforementioned phytases and the A. niger phytase.
植酸酶（EC 3.1.3.8）属于组氨酸酸性磷酸酶家族。我们已经克隆了构巢曲霉和嗜热栖热菌的植酸酶。构巢曲霉序列编码的假定酶由463个氨基酸组成，分子量为51785。嗜热栖热菌序列推导的蛋白质由466个氨基酸组成，分子量为51450。两个预测的氨基酸序列与已知植酸酶具有高度同源性（48%至67%）。这种高度同源性使得基于黑曲霉植酸酶的三维结构坐标对所有可用的真菌植酸酶进行建模成为可能。通过这种方法，我们鉴定出21个在真菌phyA植酸酶中保守的氨基酸，它们是形成底物口袋的残基的一部分。此外，还鉴定了上述植酸酶与黑曲霉植酸酶之间的潜在糖基化位点并进行了比较。
