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- W105274136 abstract "This chapter discusses intrinsic properties of zinc(II) ion pertinent to zinc enzymes. Zinc(II) ion is a biologically essential element. The crystal structure of serine/threonine phosphatase-l revealed that it contains two metal ions M(1) and M(2) close to each other. Each of the metal ions is coordinated by five ligands. The distance between the two metal ions is 3.3 Å, which is facilitated by Asp92 and a water molecule (or OH- ion); each bridges the two ions. Both metal ions and two arginine residues together create the active site. Design of useful models is, therefore, a great help in elucidating the role of metals, functions of amino acid residues, and principles of multimetal functions. The metal ions, by stabilizing negative charges, can make a phosphomonoester more susceptible to nucleophilic attack, probably by the metal-bound H2O." @default.
- W105274136 created "2016-06-24" @default.
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- W105274136 date "1996-01-01" @default.
- W105274136 modified "2023-10-17" @default.
- W105274136 title "Intrinsic Properties of Zinc(II) Ion Pertinent To Zinc Enzymes" @default.
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- W105274136 doi "https://doi.org/10.1016/s0898-8838(08)60132-4" @default.
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