Structural characteristics and catalytic mechanism of Bacillus β-propeller phytases
- 作者: Balaban N.1, Suleimanova A.1, Valeeva L.1, Shakirov E.1,2, Sharipova M.1
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隶属关系:
- Kazan (Volga Region) Federal University
- University of Texas at Austin
- 期: 卷 81, 编号 8 (2016)
- 页面: 785-793
- 栏目: Review
- URL: https://journals.rcsi.science/0006-2979/article/view/150964
- DOI: https://doi.org/10.1134/S0006297916080010
- ID: 150964
如何引用文章
详细
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.
作者简介
N. Balaban
Kazan (Volga Region) Federal University
编辑信件的主要联系方式.
Email: nellybalaban@yandex.ru
俄罗斯联邦, Kazan, 420008
A. Suleimanova
Kazan (Volga Region) Federal University
Email: nellybalaban@yandex.ru
俄罗斯联邦, Kazan, 420008
L. Valeeva
Kazan (Volga Region) Federal University
Email: nellybalaban@yandex.ru
俄罗斯联邦, Kazan, 420008
E. Shakirov
Kazan (Volga Region) Federal University; University of Texas at Austin
Email: nellybalaban@yandex.ru
俄罗斯联邦, Kazan, 420008; Austin, Texas
M. Sharipova
Kazan (Volga Region) Federal University
Email: nellybalaban@yandex.ru
俄罗斯联邦, Kazan, 420008