Download Mammalian Alkaline Phosphatases: From Biology to by José Luis Millan PDF

By José Luis Millan

A overview and dialogue of recent wisdom at the constitution and serve as of mammalian alkaline phosphatases (APs) won during the last 25 years. It covers:The constitution, law and expression of the AP genesThe 3-dimensional constitution of APs and mutagenesis paintings that additional outlined the structural/functional domain names of the isozymesThe phenotypic abnormalities of different AP knockout miceOur present figuring out of the in vivo position of the AP isozymes.The ebook additionally describes the potential use of APs as healing brokers and healing goals and the numerous makes use of of those enzymes in medical medication and in biotechnology.

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Extra resources for Mammalian Alkaline Phosphatases: From Biology to Applications in Medicine and Biotechnology

Sample text

The sequence contained within the Cys121–Cys183 disulfide bond (Fig.

The formation of the covalent enzyme–phosphate intermediate (E-P) results in inversion of the phosphorus center and the loss of the leaving group (RO–). A nucleophilic hydroxide ion coordinated to Zn1 attacks the covalent E-P intermediate, forming the noncovalent enzyme–phosphate complex (E•Pi) and causing a second inversion of configuration at the phosphorus center. The water molecule coordinated to Mg now acts as a general acid, donating a proton to Oc of Ser102 or, alternatively, inorganic phosphate.

8, all mammalian APs have five cysteine residues (Cys101, Cys121, Cys183, Cys467 and Cys474 in PLAP) per subunit, not homologous to any of the four cysteines in ECAP. They form two disulfide bonds, Cys121– Cys183 and Cys467–Cys474 (Fig. 11a), whereas the Cys101 residue remains in free form. The sequence contained within the Cys121–Cys183 disulfide bond (Fig.

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