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Literature summary extracted from

  • Neelon, K.; Wang, Y.; Stec, B.; Roberts, M.F.
    Probing the mechanism of the Archaeoglobus fulgidus inositol-1-phosphate synthase (2005), J. Biol. Chem., 280, 11475-11482.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
5.5.1.4 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
5.5.1.4 D332A site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps Archaeoglobus fulgidus
5.5.1.4 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
5.5.1.4 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
5.5.1.4 K306A site-directed mutagenesis, mutation of an active site residue, the mutant can carry out only the first 2 reaction steps Archaeoglobus fulgidus
5.5.1.4 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
5.5.1.4 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
5.5.1.4 N255A site-directed mutagenesis, mutation of a substrate binding residue, the mutant shows reduced activity Archaeoglobus fulgidus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.5.1.4 EDTA
-
 Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.5.1.4 Mg2+
-
 Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.5.1.4 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

EC Number Organism UniProt Comment Textmining
5.5.1.4 Archaeoglobus fulgidus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.5.1.4 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.5.1.4 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
-
 ?
5.5.1.4 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

EC Number Synonyms Comment Organism
5.5.1.4 inositol-1-phosphate synthase
-
 Archaeoglobus fulgidus
5.5.1.4 MIPS
-
 Archaeoglobus fulgidus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.5.1.4 90
-
 assay at Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5.1.4 7.5
-
 assay at Archaeoglobus fulgidus

Cofactor

EC Number Cofactor Comment Organism Structure
5.5.1.4 NAD+
-
 Archaeoglobus fulgidus
5.5.1.4 NADH
-
 Archaeoglobus fulgidus