The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila.
Phytases catalyse the hydrolysis of phytate (myo-inositol hexakisphosphate) to myo-inositol and inorganic phosphate. In this study genes encoding novel phytases from two different filamentous fungi, Aspergillus terreus strain 9A-1 and Myceliophthora thermophila were isolated. The encoded PhyA phytase proteins show 60% (A. terreus) and 48% (M. thermophila) identity, respectively, to the PhyA of Aspergillus niger and have 21-29% identity compared to other histidine acid phosphatases. All three PhyA proteins, in contrast to the A. niger pH 2.5-optimum acid phosphatase, prefer phytic acid as substrate and show enzyme activity at a broad range of acidic pH values. Based on their enzyme characteristics and protein sequence homology, the phytases form a novel subclass of the histidine acid phosphatase family.
Mitchell
David B
DB
Vogel
Kurt
K
Biotechnology Section, Vitamins and Fine Chemicals Division, F. Hoffmann-La Roche AG, CH-4070 Basel, Switzerland.
Weimann
Bernd J
BJ
Biotechnology Section, Vitamins and Fine Chemicals Division, F. Hoffmann-La Roche AG, CH-4070 Basel, Switzerland.
Pasamontes
Luis
L
Biotechnology Section, Vitamins and Fine Chemicals Division, F. Hoffmann-La Roche AG, CH-4070 Basel, Switzerland.
van Loon
Adolphus P G M
APGM
D010832:6-Phytase / Q000145:classification / Q000235:genetics*; D000135:Acid Phosphatase / Q000235:genetics*; D000595:Amino Acid Sequence; D001230:Aspergillus / Q000201:enzymology / Q000235:genetics; D001483:Base Sequence; D015723:Gene Library; D005800:Genes, Fungal; D003904:Mitosporic Fungi / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D000135:Acid Phosphatase; D010832:6-Phytase