Protein Variants | Comment | Organism |
---|---|---|
D225A | site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme | Archaeoglobus fulgidus |
D332A | site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps | Archaeoglobus fulgidus |
K274A | site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme | Archaeoglobus fulgidus |
K278A | site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme | Archaeoglobus fulgidus |
K306A | site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps | Archaeoglobus fulgidus |
K367A | site-directed mutagenesis, mutation of an active site residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme | Archaeoglobus fulgidus |
L257A | site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows altered D-glucose 6-phosphate binding compared to the wild-type enzyme | Archaeoglobus fulgidus |
N255A | site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows reduced activity | Archaeoglobus fulgidus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | - |
Archaeoglobus fulgidus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Archaeoglobus fulgidus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Glucose 6-phosphate | Archaeoglobus fulgidus | first step in the biosynthesis of the unusual osmolyte di-myo-inositol-1,1'-phosphate | L-myo-Inositol 1-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
D-glucose 6-phosphate = L-myo-inositol 1-phosphate | substrate binding and metal-dependent reaction mechanism, overview, active site residues are D225, K274, K278, K306, D332, and K367 | Archaeoglobus fulgidus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Glucose 6-phosphate | first step in the biosynthesis of the unusual osmolyte di-myo-inositol-1,1'-phosphate | Archaeoglobus fulgidus | L-myo-Inositol 1-phosphate | - |
? | |
D-Glucose 6-phosphate | reaction mechanism involves 3 reaction steps: 1. oxidation by NAD+, 2. condensation to a cyclic molecule, 3. reduction by NADH | Archaeoglobus fulgidus | L-myo-Inositol 1-phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
inositol-1-phosphate synthase | - |
Archaeoglobus fulgidus |
MIPS | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
90 | - |
assay at | Archaeoglobus fulgidus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Archaeoglobus fulgidus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Archaeoglobus fulgidus | |
NADH | - |
Archaeoglobus fulgidus |