myo-Inositol monophosphatase (IMP) is a soluble, Li(+)-sensitive protein that catalyzes the removal of a phosphate from myo-inositol phosphate substrates. IMP is required for de novo inositol synthesis from glucose 6-phosphate and for breakdown of inositol trisphosphate, a second messenger generated by the phosphatidylinositol signaling pathway. We cloned the IMP gene from tomato (LeIMP) and show that the plant enzyme is encoded by a small gene family. Three different LeIMP cDNAs encode distinct but highly conserved IMP enzymes that are catalytically active in vitro. Similar to the single IMP from animals, the activities of all three LeIMPs are inhibited by low concentrations of LiCl. LeIMP mRNA levels are developmentally regulated in seedlings and fruit and in response to light. Immunoblot analysis detected three proteins of distinct molecular masses (30, 29, and 28 kD) in tomato; these correspond to the predicted molecular masses of the LeIMPs encoded by the genes. Immunoreactive proteins in the same size range are also present in several other plants. Immunolocalization studies indicated that many cell types within seedlings accumulate LeIMP proteins. In particular, cells associated with the vasculature express high levels of LeIMP protein; this may indicate a coordinate regulation between phloem transport and synthesis of inositol. The presence of three distinct enzymes in tomato most likely reflects the complexity of inositol utilization in higher plants.
A unique distorted trigonal-bipyramidal geometry observed for the non-heme iron center in protocatechuate 3,4-dioxygenase (3,4-PCD) was carefully examined utilizing a sterically hindered iron salen complex, which well reproduces the endogenous His2Tyr2 donor set with water as an external ligand. X-ray crystal structures of a series of iron model complexes containing bis(3,5-dimesitylsalicylidene)-1,2-dimesitylethylenediamine indicate that a distorted trigonal-bipyramidal geometry is achieved upon binding of water as an external ligand. The extent of a structural change of the iron center from a preferred square-pyramidal to a distorted trigonal-bipyramidal geometry varies with the external ligand that is bound in the order Cl << EtO < H2O, which is consistent with the spectrochemical series. The distortion in the model system is not due to steric repulsions but electronic interactions between the external ligand and the iron center, as evidenced from the X-ray crystal structures of another series of iron model complexes with a less-hindered bis(3-xylylsalicylidene)-1,2-dimesitylethylenediamine ligand, as well as by density functional theory calculations. Further spectroscopic investigations indicate that a unique distorted trigonal-bipyramidal geometry is indeed maintained even in solution. The present model study provides a new viewpoint that a unique distorted trigonal-bipyramidal iron site might not be preorganized by a 3,4-PCD protein but could be electronically induced upon the binding of an external hydroxide ligand to the iron(III) center. The structural change induced by the external water ligand is also discussed in relation to the reaction mechanism of 3,4-PCD.
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