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Title 

Ca2+-inositol phosphate chelation mediates the substrate specificity of β-propeller phytase

Authors 

B C OhMyung Hee KimBong Sik YunW C ChoiS C ParkS C BaeTae Kwang Oh

Publisher 

American Chemical Society

Issue Date 

2006

Citation 

Biochemistry, vol. 45, no. 31, pp. 9531-9539

Keywords 

chelationphosphatessubstratesadjacent phosphate groupsinositol phosphatepropeller phytasebeta propeller phytaseinositolinositol trisphosphatephytase

Abstract 

Inositol phosphates are recognized as having diverse and critical roles in biological systems. In this report, kinetic studies and TLC analysis indicate that β-propeller phytase is a special class of inositol phosphatase that preferentially recognizes a bidentate (P-Ca2+-P) formed between Ca2+ and two adjacent phosphate groups of its natural substrate phytate (InsP6). The specific recognition of a bidentate chelation enables the enzyme to sequentially hydrolyze one of the phosphate groups in a bidentate of Ca2+-InsP6 to yield a myo-inositol trisphosphate (InsP3) and three phosphates as the final products. A comparative analysis of 1H- and 13C NMR spectroscopy with the aid of 2D NMR confirms that the chemical structure of the final product is wyo-Ins(2,4,6)P3. The catalytic properties of the enzyme suggest a potential model for how the enzyme specifically recognizes its substrate Ca 2+-InsP6 and produces myo-Ins(2,4,6)-P3 from Ca2+-InsP6- These findings potentially provide evidence for a selective Ca2+-InsP6 chelation between Ca 2+ and two adjacent phosphate groups of inositol phosphates.

ISSN 

0006-2960

Link 

http://dx.doi.org/10.1021/bi0603118

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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