Structural characteristics and catalytic mechanism of Bacillus β-propeller phytases
- Authors: Balaban N.P.1, Suleimanova A.D.1, Valeeva L.R.1, Shakirov E.V.1,2, Sharipova M.R.1
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Affiliations:
- Kazan (Volga Region) Federal University
- University of Texas at Austin
- Issue: Vol 81, No 8 (2016)
- Pages: 785-793
- Section: Review
- URL: https://journals.rcsi.science/0006-2979/article/view/150964
- DOI: https://doi.org/10.1134/S0006297916080010
- ID: 150964
Cite item
Abstract
ß-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 ß-propeller phytases of calcium complexes with myo-inositol hexakisphosphate.
About the authors
N. P. Balaban
Kazan (Volga Region) Federal University
Author for correspondence.
Email: nellybalaban@yandex.ru
Russian Federation, Kazan, 420008
A. D. Suleimanova
Kazan (Volga Region) Federal University
Email: nellybalaban@yandex.ru
Russian Federation, Kazan, 420008
L. R. Valeeva
Kazan (Volga Region) Federal University
Email: nellybalaban@yandex.ru
Russian Federation, Kazan, 420008
E. V. Shakirov
Kazan (Volga Region) Federal University; University of Texas at Austin
Email: nellybalaban@yandex.ru
Russian Federation, Kazan, 420008; Austin, Texas
M. R. Sharipova
Kazan (Volga Region) Federal University
Email: nellybalaban@yandex.ru
Russian Federation, Kazan, 420008