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

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Title
Ca2+-inositol phosphate chelation mediates the substrate specificity of β-propeller phytase
Author(s)
B C Oh; Myung Hee Kim; Bong Sik Yun; W C Choi; S C Park; S C Bae; Tae Kwang Oh
Bibliographic Citation
Biochemistry, vol. 45, no. 31, pp. 9531-9539
Publication Year
2006
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
Publisher
Amer Chem Soc
DOI
http://dx.doi.org/10.1021/bi0603118
Type
Article
Appears in Collections:
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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