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

<div>Structural model of<i> Wickerhamomyces anomalus</i> phytase proposed by Kaur et al. [<a href="/journals/er/2018/8240698/#B55">54</a>] available at <a href="https://www.ncbi.nlm.nih.gov/protein">https://www.ncbi.nlm.nih.gov/protein</a> and i-TASSER server used for protein structure and function prediction (<a href="https://zhanglab.ccmb.med.umich.edu/I-TASSER/">https://zhanglab.ccmb.med.umich.edu/I-TASSER/</a>) [<a href="/journals/er/2018/8240698/#B59">105</a>]. The domains are identified in the secondary structure elements being alpha-helices (1) and the secondary structure (2).</div>

Enzyme Research

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Figure 5

Figure 5: Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications 

Figure 5 | Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications 