scholarly journals Isolation, partial purification and biochemical characterization of chloroplastic L-myo-inositol-1-phosphate synthase from a macro alga Enteromorpha intestinalis under high salinity

2018 ◽  
Vol 16 (1) ◽  
pp. 21-30
Keyword(s):  
Biochemical Characterization ◽  
High Salinity ◽  
Partial Purification ◽  
Enteromorpha Intestinalis ◽  
Inositol 1 ◽  
Phosphate Synthase

Partial purification and characterization of rat brain myo-inositol-1-phosphatase

1987 ◽  
Vol 15 (3) ◽  
pp. 429-430 ◽  
Author(s):  
F. CAREY ◽  
J. A. CREBA ◽  
P. J. FRENCH ◽  
A. D. SHORT ◽  
M. WALTERS ◽  
...  
Keyword(s):  
Rat Brain ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Inositol 1

Functional characterization of two myo-inositol-1-phosphate synthase (MIPS) gene promoters from the halophytic wild rice (Porteresia coarctata)

Planta ◽  
2018 ◽  
Vol 248 (5) ◽  
pp. 1121-1141 ◽  
Author(s):  
Papri Basak ◽  
Shiny Sangma ◽  
Abhishek Mukherjee ◽  
Tanushree Agarwal ◽  
Sonali Sengupta ◽  
...  
Keyword(s):  
Wild Rice ◽  
Functional Characterization ◽  
Gene Promoters ◽  
Porteresia Coarctata ◽  
Inositol 1 ◽  
Phosphate Synthase

scholarly journals The INO2 and INO4 loci of Saccharomyces cerevisiae are pleiotropic regulatory genes.

1984 ◽  
Vol 4 (11) ◽  
pp. 2479-2485 ◽  
Author(s):  
B S Loewy ◽  
S A Henry
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Gene Product ◽  
Regulatory Genes ◽  
Wild Type ◽  
Inositol 1 ◽  
Cytoplasmic Enzyme ◽  
Pleiotropic Phenotype ◽  
Reduced Rate ◽  
Phosphate Synthase

We isolated a mutant of Saccharomyces cerevisiae defective in the formation of phosphatidylcholine via methylation of phosphatidylethanolamine. The mutant synthesized phosphatidylcholine at a reduced rate and accumulated increased amounts of methylated phospholipid intermediates. It was also found to be auxotrophic for inositol and allelic to an existing series of ino4 mutants. The ino2 and ino4 mutants, originally isolated on the basis of an inositol requirement, are unable to derepress the cytoplasmic enzyme inositol-1-phosphate synthase (myo-inositol-1-phosphate synthase; EC 5.5.1.4). The INO4 and INO2 genes were, thus, previously identified as regulatory genes whose wild-type product is required for expression of the INO1 gene product inositol-1-phosphate synthase (T. Donahue and S. Henry, J. Biol. Chem. 256:7077-7085, 1981). In addition to the identification of a new ino4-allele, further characterization of the existing series of ino4 and ino2 mutants, reported here, demonstrated that they all have a reduced capacity to convert phosphatidylethanolamine to phosphatidylcholine. The pleiotropic phenotype of the ino2 and ino4 mutants described in this paper suggests that the INO2 and INO4 loci are involved in the regulation of phospholipid methylation in the membrane as well as inositol biosynthesis in the cytoplasm.

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