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Ester transfication by Ni(II) hydroxy complex by Masami Ito; Yu-saku Takita is a Chemistry article available to read on EtoBox.
What is Ester transfication by Ni(II) hydroxy complex about?
Alkaline phosphatase catalyzes the phosphates hydrolysis and ester transfication under the presence of external alcohol 1. This enzyme contains two Zn(II) ion and one Mg(II) ion at the active site, and it is believed that the key intermediate Zn(II)-OH-is afforded by the deprotonation of the Zn(II)-bound water. While the metal hydroxy moiety can be the good candidate for the nucleophilic attack toward the ester, there is one serine residue adjacent to the Zn(II) ion and that amino acid residue may have a significant roll for the catalytic reaction in this enzyme. In the case of none-metal hydrolytic enzyme, such as chymotrypsin, the alcoholic OH in serine residue works as the nucleophile activated by an adjacent imidazole 2. The reaction of the "activated" serine in chymotrypsin with ester affords the acyl intermediate, finally the hydrolysis reaction of the acyl intermediate occurs by the external water. Therefore, as the roll of serine residue in alkaline phosphatase is not clear, the established reaction mechanism of alkaline phosphatase does not exist at the present stage. Kimura et. al. propose that the alcohol residue can be activated by the hydrogen bond with the Zn(II)-boun
Who reads Ester transfication by Ni(II) hydroxy complex?
It is typically read by researchers, students, and practitioners in Chemistry.
- Author
- Masami Ito; Yu-saku Takita
- Publisher
- Elsevier Science; Elsevier ; Elsevier BV (ISSN 0162-0134)
- Published
- 1997
- Language
- EN
- Field
- Chemistry (Physical Sciences)