NDLI: Metal ion induced allosteric transition in the catalytic activity of an artificial phosphodiesterase

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Organic & Biomolecular Chemistry Vol -5

Organic & Biomolecular Chemistry Vol -4

Organic & Biomolecular Chemistry Vol -3

Organic & Biomolecular Chemistry Vol -2

Metal ion induced allosteric transition in the catalytic activity of an artificial phosphodiesterase

Content Provider	Royal Society of Chemistry (RSC)
Author	Takeuchi, Masayuki Ikeda, Masato Shinkai, Seiji Takebayashi, Shinji
Copyright Year	2008
Abstract	An artificial phosphodiesterase (1) bearing two types of metal binding sites, a catalytic site and a regulatory bipyridine site showed a unique allosteric transition in the catalytic activity against the metal concentration. The rate constants for the hydrolysis reaction of 2-hydroxypropyl-p-nitrophenyl phosphate (HPNP) and RNA dimer (ApA) with and without an effector metal ion were evaluated; the kobs value of HPNP hydrolysis for 1·(Zn2+)3 (2.0 × 10−4 s−1) is 3.3 times larger than that for 1·(Zn2+)2. In the case of 1 and Cu2+, a 19.4 times larger kobs value was obtained for 1·(Cu2+)3 (1.2 × 10−3 s−1) against 1·(Cu2+)2. The increase in the catalytic activity is ascribed to the allosteric conformational transition of 1 induced by the coordination of effector metal ion to the Bpy moiety. A detailed investigation revealed that a conformational change of 1 induced by the third M2+ complexation enhances the rate of hydrolysis rather than a change in the substrate affinity.
Starting Page	493
Ending Page	499
Page Count	7
File Format	HTM / HTML PDF
ISSN	14770520
Volume Number	6
Issue Number	3
Journal	Organic & Biomolecular Chemistry
DOI	10.1039/b716196d
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Hydrolysis Allosteric regulation RNA Bipyridine Phosphate Ion Protein dimer Phosphodiesterase
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Physical and Theoretical Chemistry

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