Structural characteristics and catalytic mechanism of Bacillus β-propeller phytases

被引：12

作者：

Balaban, N. P. ^{[1
]}

Suleimanova, A. D. ^{[1
]}

Valeeva, L. R. ^{[1
]}

Shakirov, E. V. ^{[1
,2
]}

Sharipova, M. R. ^{[1
]}

机构：

[1] Kazan Volga Reg Fed Univ, Kazan 420008, Russia

[2] Univ Texas Austin, Austin, TX 78712 USA

来源：

BIOCHEMISTRY-MOSCOW | 2016年 / 81卷 / 08期

基金：

俄罗斯基础研究基金会;

关键词：

beta-propeller phytases; calcium-binding site; myo-inositol hexakisphosphate; calcium-phytate complex; catalytic mechanism; PURPLE ACID-PHOSPHATASES; CRYSTAL-STRUCTURES; ALKALINE PHYTASE; THERMOSTABLE PHYTASE; SPECIFICITY; ELUCIDATION; COMPLEX; SITE;

D O I：

10.1134/S0006297916080010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

-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 -propeller phytases of calcium complexes with myo-inositol hexakisphosphate.

引用

页码：785 / 793

页数：9

共 38 条

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