Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications

Figure 2

Structural model of purple acid phosphatase from barley (Hordeum vulgare) proposed by Dionisio et al. [4]. PAPhy genes are grouped in isogenes HvPAPhy_a, HvPAPhy_b1, and HvPAPhy_b2. Isogenes HvPAPhy possess significant phytase activity in the mature grains and proteins already were produced in P. pastoris. Structural model used i-TASSER server for protein structure and function prediction (https://zhanglab.ccmb.med.umich.edu/I-TASSER/) [105]. FASTA sequences were obtained from https://www.ncbi.nlm.nih.gov/protein. Isoform a is constituted by 544 amino acids, 60,29 kDa, and Hphob of 49,5%. The ligand-binding site residues from isoform a are represented by amino acid sequence 199, 226, 283, 365, and 402. Isoform b1 is constituted by 536 amino acids and 59,51 kDa with the ligand-binding site residues being represented by amino acid sequence 194, 221, 278, 359, and 396. Isoform b2 is constituted by 537 amino acids and 59,34 kDa. Ligand-binding site residues are constituted by amino acid sequence 194, 221, 278, 360, and 397.