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- W2074480260 endingPage "1142" @default.
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- W2074480260 abstract "Myo-inositol monophosphatase is a pivotal enzyme of the inositol second messenger system which is specifically inhibited by therapeutic levels of lithium salts, implicating inhibition of this enzyme as a potential site of its action in bipolar disease. This enzyme has a native molecular weight of 59,000, and has traditionally been found in the cytosolic fraction, although a membrane-bound form has also been identified. Possessing two identical subunits, this enzyme hydrolyzes those monophosphates which are equatorially located within the inositol ring, and several nucleoside monophosphates phosphorylated at the 2-position. Each subunit of the native enzyme contains an active site with unusually large caverns as revealed by crystallographic studies, which may explain the accommodation of these structurally unrelated substrates. We have suggested that the uncompetitive inhibition of this phosphatase by lithium ions may prevent the formation of an enzyme-bound non-isomeric (meso) intermediate, Mg(2+)-inositol 1,3 or 4,6 cyclic monophosphate when this enzyme hydrolyzes its respective isomeric substrates." @default.
- W2074480260 created "2016-06-24" @default.
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- W2074480260 creator A5028449471 @default.
- W2074480260 creator A5043123629 @default.
- W2074480260 creator A5091530017 @default.
- W2074480260 date "1994-01-01" @default.
- W2074480260 modified "2023-09-25" @default.
- W2074480260 title "Biochemical and molecular properties of lithium-sensitive myo-inositol monophosphatase" @default.
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- W2074480260 doi "https://doi.org/10.1016/0024-3205(94)00835-3" @default.
- W2074480260 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8152337" @default.
- W2074480260 hasPublicationYear "1994" @default.
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