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D225A
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site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
D332A
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site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps
K274A
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site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
K278A
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site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
K306A
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site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps
K367A
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site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
L257A
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site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme
N255A
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site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows reduced activity
DELTAD342
the mutant shows 75% of wild type activity
DELTAD422
the mutant shows 73% of wild type activity
DELTAI386
the mutant shows 79% of wild type activity
DELTAK355/DELTAK359
the mutant shows 7% of wild type activity
DELTAK359
the mutant shows 59% of wild type activity
DELTAL346
the mutant shows 90% of wild type activity
DELTAV384
the mutant shows 59% of wild type activity
K355A/K359A
the mutant shows 14% of wild type activity
K369A
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mutation results in complete loss of activity
K369A
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site-directed mutagenesis, mutant shows altered substrate and inhibitor binding
K412A
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mutation results in complete loss of activity
K412A
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site-directed mutagenesis, mutant shows altered substrate and inhibitor binding
K489A
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mutation results in complete loss of activity
K489A
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site-directed mutagenesis, mutant shows altered substrate and inhibitor binding
additional information
construction of transgenic plants expressing GFP-tagged MIPS using Agrobacterium tumefaciens GV3101 transfection method, overview
additional information
single mips mutants show no obvious phenotypes, but mips1 mips2 double mutant and the mips1 mips2 mips3 triple mutant are embryo lethal, whereas the mips1 mips3 and mips1 mips2+/- double mutants has abnormal embryos. The double and triple mips mutants display abnormal expression patterns of DR5:GFP, an auxin-responsive fusion protein, and they have altered PIN1 subcellular localization. Also, membrane trafficking is affected in mips1 mips3, overview. overexpression of phosphatidylinositol synthase 2, which converts myoinositol to membrane phosphatidylinositol, largely rescued the cotyledon and endomembrane defects in mips1 mips3
additional information
single mips mutants show no obvious phenotypes, but mips1 mips2 double mutant and the mips1 mips2 mips3 triple mutant are embryo lethal, whereas the mips1 mips3 and mips1 mips2+/- double mutants has abnormal embryos. The double and triple mips mutants display abnormal expression patterns of DR5:GFP, an auxin-responsive fusion protein, and they have altered PIN1 subcellular localization. Also, membrane trafficking is affected in mips1 mips3, overview. overexpression of phosphatidylinositol synthase 2, which converts myoinositol to membrane phosphatidylinositol, largely rescued the cotyledon and endomembrane defects in mips1 mips3
additional information
single mips mutants show no obvious phenotypes, but mips1 mips2 double mutant and the mips1 mips2 mips3 triple mutant are embryo lethal, whereas the mips1 mips3 and mips1 mips2+/- double mutants has abnormal embryos. The double and triple mips mutants display abnormal expression patterns of DR5:GFP, an auxin-responsive fusion protein, and they have altered PIN1 subcellular localization. Also, membrane trafficking is affected in mips1 mips3, overview. overexpression of phosphatidylinositol synthase 2, which converts myoinositol to membrane phosphatidylinositol, largely rescued the cotyledon and endomembrane defects in mips1 mips3
additional information
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single mips mutants show no obvious phenotypes, but mips1 mips2 double mutant and the mips1 mips2 mips3 triple mutant are embryo lethal, whereas the mips1 mips3 and mips1 mips2+/- double mutants has abnormal embryos. The double and triple mips mutants display abnormal expression patterns of DR5:GFP, an auxin-responsive fusion protein, and they have altered PIN1 subcellular localization. Also, membrane trafficking is affected in mips1 mips3, overview. overexpression of phosphatidylinositol synthase 2, which converts myoinositol to membrane phosphatidylinositol, largely rescued the cotyledon and endomembrane defects in mips1 mips3
additional information
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construction of transgenic plants expressing GFP-tagged MIPS using Agrobacterium tumefaciens GV3101 transfection method, overview
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additional information
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the human enzyme can functionally complement the enzyme-deficient Saccharomyces cerevisiae ino1 mutant strain
additional information
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significant reduction of enzyme expression by use of phosphorothioate-modified antisense oligodeoxyribonucleotides. Treatment results in reduced level of mycothiol and the proliferation of Mycobacterium tuberculosis, enhanced susceptibility to antibiotics isoniazid, vancomycin and rifampin and decreased tolerance to H2O2
additional information
A 37-amino acid stretch between W174 and S210 is the salt-tolerance determinant domain of enzyme. Deletion of this stretch results in loss of salt tolerance, introduction of stretch into Brassica juncea or Oryza sativa enzyme provides salt tolerance properties
additional information
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A 37-amino acid stretch between W174 and S210 is the salt-tolerance determinant domain of enzyme. Deletion of this stretch results in loss of salt tolerance, introduction of stretch into Brassica juncea or Oryza sativa enzyme provides salt tolerance properties
additional information
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functional introgression of enzyme gene confers salt-tolerance to several organisms such as Escherichia coli, Schizosaccharomyces pombe, Oryza sativa and Brassica juncea albeit to varialbe extent. Direct correlation between increased synthesis of inositol under salinity stress by the enzyme and salt tolerance
additional information
a 37-amino acid stretch between W174 and S210 is the salt-tolerance determinant domain of Porteresia coarctata enzyme. Introduction of this stretch into Oryza sativa enzyme provides salt tolerance properties
additional information
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the enzyme-deficient ino1 mutant strain can be functionally complemented by expression of the human enzyme
additional information
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the enzyme-deficient Saccharomyces cerevisiae ino1 mutant strain FY250 can be functionally complemented by expression of sll1722
additional information
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enzyme gene can complement inositol auxotroph Saccharomyces cerevisiae strain FY250 and the natural inositol auxotroph Schizosaccharomyces pombe
additional information
maize mutant ipa 1-1 produces kernels containing low phytic acid, reducd by 66% compared to the wild-type maize kernels probably due to a mutation in the gene encoding the enzyme, i.e. gene MIPS, overview
additional information
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maize mutant ipa 1-1 produces kernels containing low phytic acid, reducd by 66% compared to the wild-type maize kernels probably due to a mutation in the gene encoding the enzyme, i.e. gene MIPS, overview