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Inositol monophosphatase is a highly conserved enzyme having localized structural similarity to both glycerol 3-phosphate dehydrogenase and haemoglobin.
Wreggett KA
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The cDNA coding for an inositol monophosphatase in the oocytes of the African clawed frog, Xenopus laevis, has been isolated and sequenced. The predicted primary structure of this enzyme is markedly conserved when it is compared with its mammalian functional homologues; up to 84% of the amino acid residues are identical, and conservative substitutions increase the similarity to 95%, suggesting that this sequence represents the most parsimonious primary structure for the protein to maintain not only catalytic activity but also perhaps the facility to interact with other macromolecules. Two regions of the protein, each of about 11 residues and separated by about 90 residues, have been identified as a consensus found also in glycerol 3-phosphate dehydrogenase (EC 1.1.1.8). One of these regions is also found to be particularly conserved in the alpha-globin of birds and reptiles; birds and some turtles are known to modulate the oxygen affinity of their haemoglobin with inositol polyphosphate in the same way as with 2,3-bisphosphoglycerate in other species. This region is also conserved in the beta-globin of most species, beginning with lysine-82, which is known to participate in the binding of organic phosphates. These regions of the inositol monophosphatase may represent motifs for the binding of its substrate.
Arnone,
Structure of inositol hexaphosphate--human deoxyhaemoglobin complex.
1974, Pubmed
Arnone,
Structure of inositol hexaphosphate--human deoxyhaemoglobin complex.
1974,
Pubmed
Arnone,
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin.
1972,
Pubmed
Bartlett,
Isolation and assay of red-cell inositol polyphosphates.
1982,
Pubmed
Berridge,
Lithium amplifies agonist-dependent phosphatidylinositol responses in brain and salivary glands.
1982,
Pubmed
Berridge,
Neural and developmental actions of lithium: a unifying hypothesis.
1989,
Pubmed
Busa,
Roles for the phosphatidylinositol cycle in early development.
1988,
Pubmed
Busa,
Lithium-induced teratogenesis in frog embryos prevented by a polyphosphoinositide cycle intermediate or a diacylglycerol analog.
1989,
Pubmed
,
Xenbase
Collins,
The significance of protein sequence similarities.
1988,
Pubmed
Devereux,
A comprehensive set of sequence analysis programs for the VAX.
1984,
Pubmed
Diehl,
Cloning and expression of bovine brain inositol monophosphatase.
1990,
Pubmed
Duguet,
Phylogeny of hemoglobins: the complete amino acid sequence of an alpha-chain of viper (Vipera aspis) hemoglobin.
1974,
Pubmed
Fabiny,
Ammonium transport in Escherichia coli: localization and nucleotide sequence of the amtA gene.
1991,
Pubmed
Gee,
The purification and properties of myo-inositol monophosphatase from bovine brain.
1988,
Pubmed
Hallcher,
The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain.
1980,
Pubmed
Isaacks,
Studies on avian erythrocyte metabolism. Inositol tetrakisphosphate: the major phosphate compound in the erythrocytes of the ostrich (Struthio camelus camelus).
1977,
Pubmed
Kozak,
The scanning model for translation: an update.
1989,
Pubmed
McAllister,
cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme.
1992,
Pubmed
Natsumeda,
Two distinct cDNAs for human IMP dehydrogenase.
1990,
Pubmed
Pearson,
Improved tools for biological sequence comparison.
1988,
Pubmed
Saunders,
Rapid isolation of miniprep DNA for double strand sequencing.
1990,
Pubmed
Watanabe,
Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells.
1989,
Pubmed
Yelton,
Identification and nucleotide sequence of the Leptospira biflexa serovar patoc trpE and trpG genes.
1989,
Pubmed