Metal ion induced allosteric transition in the catalytic activity of an artificial phosphodiesterase.
An artificial phosphodiesterase (1) bearing two kinds 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.
Takebayashi
Shinji
S
Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka 812-8581, Japan.
Ikeda
Masato
M
Takeuchi
Masayuki
M
Shinkai
Seiji
S
D000494:Allosteric Regulation; D000495:Allosteric Site; D002384:Catalysis; D002413:Cations, Divalent / Q000737:chemistry; D003300:Copper / Q000737:chemistry*; D007700:Kinetics; D015394:Molecular Structure; D010727:Phosphoric Diester Hydrolases / Q000138:chemical synthesis* / Q000737:chemistry; D015032:Zinc / Q000737:chemistry*
D002413:Cations, Divalent; D003300:Copper; D010727:Phosphoric Diester Hydrolases; D015032:Zinc