phytic acid and inositol 1-phosphate

phytic acid has been researched along with inositol 1-phosphate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Broger, C; Brugger, R; Pasamontes, L; Schnoebelen, L; Tessier, M; Tomschy, A; van Loon, AP; Wyss, M	1
Islas-Flores, I; Villanueva, MA	1

Other Studies

2 other study(ies) available for phytic acid and inositol 1-phosphate

Article	Year
Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure. Protein science : a publication of the Protein Society, 2000, Volume: 9, Issue:7 Topics: 6-Phytase; Amino Acid Sequence; Amino Acid Substitution; Aspergillus fumigatus; Aspergillus niger; Base Sequence; Catalytic Domain; Enzyme Stability; Hydrogen-Ion Concentration; Inositol Phosphates; Molecular Sequence Data; Phytic Acid; Point Mutation; Protein Conformation; Protein Engineering	2000
Inositol-1 (or 4)-monophosphatase from Glycine max embryo axes is a phosphatase with broad substrate specificity that includes phytate dephosphorylation. Biochimica et biophysica acta, 2007, Volume: 1770, Issue:4 Topics: Adenosine Triphosphate; Amino Acid Sequence; Cations, Divalent; Diphosphates; Enzyme Induction; Enzyme Stability; Germination; Glycine max; Hot Temperature; Hydrolysis; Inositol Phosphates; Kinetics; Lithium Chloride; Molecular Sequence Data; Molecular Weight; Phosphoric Monoester Hydrolases; Phosphorylation; Phytic Acid; Protein Denaturation; Seeds; Sodium Fluoride; Substrate Specificity; Time Factors	2007

Article

Year

Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure.

Protein science : a publication of the Protein Society, 2000, Volume: 9, Issue:7

Topics: 6-Phytase; Amino Acid Sequence; Amino Acid Substitution; Aspergillus fumigatus; Aspergillus niger; Base Sequence; Catalytic Domain; Enzyme Stability; Hydrogen-Ion Concentration; Inositol Phosphates; Molecular Sequence Data; Phytic Acid; Point Mutation; Protein Conformation; Protein Engineering

2000

Inositol-1 (or 4)-monophosphatase from Glycine max embryo axes is a phosphatase with broad substrate specificity that includes phytate dephosphorylation.

Biochimica et biophysica acta, 2007, Volume: 1770, Issue:4

Topics: Adenosine Triphosphate; Amino Acid Sequence; Cations, Divalent; Diphosphates; Enzyme Induction; Enzyme Stability; Germination; Glycine max; Hot Temperature; Hydrolysis; Inositol Phosphates; Kinetics; Lithium Chloride; Molecular Sequence Data; Molecular Weight; Phosphoric Monoester Hydrolases; Phosphorylation; Phytic Acid; Protein Denaturation; Seeds; Sodium Fluoride; Substrate Specificity; Time Factors

2007