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REVIEW: Structural Characteristics and Catalytic Mechanism of Bacillus β-Propeller Phytases

N. P. Balaban1*, A. D. Suleimanova1, L. R. Valeeva1, E. V. Shakirov1,2, and M. R. Sharipova1

1Kazan (Volga Region) Federal University, 420008 Kazan, Russia; E-mail: nellybalaban@yandex.ru

2University of Texas at Austin, Austin, Texas, USA

* To whom correspondence should be addressed.

Received December 17, 2015; Revision received May 4, 2016
β-Propeller phytases of Bacillus are unique highly conservative and highly specific enzymes capable of cleaving insoluble phytate compounds. In this review, we analyzed data on the properties of these enzymes, their differences from other phytases, and their unique spatial structures and substrate specificities. We considered influences of different factors on the catalytic activity and thermostability of these enzymes. There are few data on the hydrolysis mechanism of these enzymes, which makes it difficult to analyze their mechanism of action and their final products. We analyzed the available data on hydrolysis by β-propeller phytases of calcium complexes with myo-inositol hexakisphosphate.
KEY WORDS: β-propeller phytases, calcium-binding site, myo-inositol hexakisphosphate, calcium–phytate complex, catalytic mechanism

DOI: 10.1134/S0006297916080010