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Annegrit Seifried, Jörg Schultz and Antje Gohla Human HAD phosphatases: structure, mechanism, and roles in health and disease The FEBS Journal 280

Version of Record online: 13 JUN 2012 | DOI: 10.1111/j.1742-4658.2012.08633.x

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Phosphatases of the haloacid dehalogenase (HAD) superfamily can exhibit exquisite substrate specificities. These phosphatases have undergone a remarkable expansion during metazoan evolution, and some have acquired an elaborate extracatalytic multidomain structure. In this review, we describe the gene complement of human HAD phosphatases, discuss their structure, catalytic mechanism and evolution, and summarize their known functions in health and disease.

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